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Bertini, I., Calderone, V., Fragai, M., Luchinat, C., Maletta, M., Yeo, K.J.(2006) Angew Chem Int Ed Engl 45: 7952-7955
2OY2
Human MMP-8 in complex with peptide IAG
- PDB DOI: https://doi.org/10.2210/pdb2OY2/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2007-02-21 Released: 2007-03-06
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.192
- R-Value Work: 0.164
- R-Value Observed: 0.166
wwPDB Validation 3D Report Full Report
This is version 1.4 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Neutrophil collagenase | A, C [auth F] | 158 | Homo sapiens | Mutation(s): 0 Gene Names: MMP8, CLG1 EC: 3.4.24.34 |  |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P22894 (Homo sapiens) Explore P22894 Go to UniProtKB: P22894 | |||||
PHAROS: P22894 GTEx: ENSG00000118113 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P22894 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| ILE-ALA-GLY peptide | B [auth W], D [auth Y] | 3 | N/A | Mutation(s): 0 |  |
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ZN Query on ZN | G [auth A], H [auth A], K [auth F], L [auth F] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| CA Query on CA | E [auth A], F [auth A], I [auth F], J [auth F] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.192
- R-Value Work: 0.164
- R-Value Observed: 0.166
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 33.207 | α = 90 |
| b = 68.533 | β = 98.1 |
| c = 78.281 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MAR345 | data collection |
| MOSFLM | data reduction |
| CCP4 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2007-03-06 Deposition Author(s): Calderone, V., Bertini, I., Fragai, M., Luchinat, C., Maletta, M., Yeo, K.J.
Revision History (Full details and data files)
- Version 1.0: 2007-03-06
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-10-18
Changes: Refinement description - Version 1.4: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description
