Download MendeleyFirst-principles calculation of pseudo-contact shifts in a paramagnetic metalloprotein
Benda, L., Mares, J., Ravera, E., Parigi, G., Luchinat, C., Kaupp, M., Vaara, J.To be published.
5LAB
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
- PDB DOI: https://doi.org/10.2210/pdb5LAB/pdb
- Entry: 5LAB supersedes: 1RMZ
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2016-06-14 Released: 2016-08-10
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.34 Å
- R-Value Free: 0.195
- R-Value Work: 0.155
- R-Value Observed: 0.158
Starting Model: experimental
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This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Macrophage metalloelastase | 159 | Homo sapiens | Mutation(s): 1 Gene Names: MMP12, HME EC: 3.4.24.65 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P39900 (Homo sapiens) Explore P39900 Go to UniProtKB: P39900 | |||||
PHAROS: P39900 GTEx: ENSG00000262406 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P39900 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NGH Query on NGH | G [auth A] | N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID C13 H20 N2 O5 S JIRXORZYIXSWOB-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | B [auth A], C [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| CA Query on CA | D [auth A], E [auth A], F [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.34 Å
- R-Value Free: 0.195
- R-Value Work: 0.155
- R-Value Observed: 0.158
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 69.19 | α = 90 |
| b = 62.56 | β = 90 |
| c = 37.26 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2016-08-10 Deposition Author(s): Ravera, E., Calderone, V., Luchinat, C.
- This entry supersedes: 1RMZ
Revision History (Full details and data files)
- Version 1.0: 2016-08-10
Type: Initial release - Version 1.1: 2024-02-07
Changes: Data collection, Database references, Refinement description
