MolNFT v1 · #147704 · protein
Crystal structure of MMP12 in complex with inhibitor BE4.
6ELA: “Crystal structure of MMP12 in complex with inhibitor BE4.”. X-ray diffraction, 3 ligands (B9Z, CA, ZN). MolNFT v1 #147704 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6ELA
- Type
- protein
- Length
- 631 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39900
- Ligands
- B9Z, CA, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 157 | — | P39900 |
| B, C, D | — | protein | 158 | — | P39900 |
Ligands and binding sites
- B9Z · (2~{S})-2-[2-[4-(4-methoxyphenyl) phenyl]sulfanylphenyl]pentanedioic acid · ligand · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 12 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
- DIO · 1,4-diethylene dioxide · additive · 5 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ELA · Crystal structure of MMP12 in complex with inhibitor BE4. · the same entry in another collection · chain A against A, TM-score 1.00
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 P39900
- Elsewhere: RCSB PDB 6ELA · PDBe 6ELA · UniProt P39900
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