2F6A

Collagen Adhesin and Collagen Complex Structure

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Bacterial adhesin-like	8040195	3000723	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Bacterial adhesin-like	8040195	3000723	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Bacterial adhesin-like	8040195	3000723	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Bacterial adhesin-like	8040195	3000723	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Collagen_bind	e2f6aA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Collagen_bind	ECOD (1.6)
A	Candida_ALS_N_like_1	e2f6aA2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Candida_ALS_N_like_1	ECOD (1.6)
B	Collagen_bind	e2f6aB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Collagen_bind	ECOD (1.6)
B	Candida_ALS_N_like_1	e2f6aB2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Candida_ALS_N_like_1	ECOD (1.6)
C	Collagen_bind	e2f6aC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Collagen_bind	ECOD (1.6)
C	Candida_ALS_N_like_1	e2f6aC2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Candida_ALS_N_like_1	ECOD (1.6)
D	Collagen_bind	e2f6aD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Collagen_bind	ECOD (1.6)
D	Candida_ALS_N_like_1	e2f6aD2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Common fold of diphtheria toxin/transcription factors/cytochrome f	F: Candida_ALS_N_like_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1280	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	2.60.40.740	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
B	2.60.40.1280	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
B	2.60.40.740	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
C	2.60.40.1280	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
C	2.60.40.740	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
D	2.60.40.1280	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
D	2.60.40.740	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF05737	Collagen binding domain (Collagen_bind)	Collagen binding domain	The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices [1]. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence pre ...	The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices [1]. A groove on beta-sheet I exhibited the best surface complementarity to the collagen. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen.	Domain
E, F, G, H, I E, F, G, H, I, J	PF01391	Collagen triple helix repeat (20 copies) (Collagen)	Collagen triple helix repeat (20 copies)	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Collagen adhesin	collagen binding protein-containing complex binding binding	cell adhesion cellular process	cell periphery cellular anatomical structure external encapsulating structure cell wall peptidoglycan-based cell wall extracellular region
E, F, G, H, I E, F, G, H, I, J	Collagen	structural molecule activity extracellular matrix structural constituent extracellular matrix structural constituent conferring tensile strength	cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization	cellular anatomical structure membrane extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B, C, D	IPR008456	Collagen binding domain	Domain
A, B, C, D	IPR008454	Collagen-binding surface protein Cna-like, B-type domain	Domain
A, B, C, D	IPR041033	SpaA-like, prealbumin fold domain subgroup 1	Domain
A, B, C, D	IPR008966	Adhesion domain superfamily	Homologous Superfamily
A, B, C, D	IPR011252	Fibrogen-binding domain 1	Homologous Superfamily
A, B, C, D	IPR019931	LPXTG cell wall anchor domain	Domain
E, F, G, H, I E, F, G, H, I, J	IPR008160	Collagen triple helix repeat	Repeat
E, F, G, H, I E, F, G, H, I, J	IPR017095	Saimiri transformation-associated protein	Family
E, F, G, H, I E, F, G, H, I, J	IPR050149	Collagen superfamily	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
E, F, G, H, I E, F, G, H, I, J	HYP	Parent Component: PRO RESID: AA0030 PSI-MOD : 4-hydroxy-L-proline MOD:00039

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.