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Crystal structure of MMP8 complexed with HMR2909
Analyse Crystal structure of MMP8 complexed with HMR2909 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BZS
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neutrophil collagenase
- EC
- 3.4.24.34
- UniProt
- P22894
- Ligands
- BSI, CA, ZN
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neutrophil collagenase (EC 3.4.24.34) | protein | 165 | 24% helix, 16% strand | P22894 |
Ligands and binding sites
- BSI · 2-(biphenyl-4-sulfonyl)-1,2,3,4-tetrahydro-isoquinoline-3-carboxylic acid · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.52 | 0.82 | 24 | ZN, BSI |
| 2 | 54 | 0.30 | 0.75 | 19 | EPE |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P22894
- Elsewhere: RCSB PDB 1BZS · PDBe 1BZS · UniProt P22894
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