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Crystal structure of MMP9 in complex with inhibitor BE4.
Analyse Crystal structure of MMP9 in complex with inhibitor BE4. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ESM
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix metalloproteinase-9,MATRIX metalloproteinase-9
- EC
- 3.4.24.35
- UniProt
- P14780
- Ligands
- B9Z, PZE, CA, ZN
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix metalloproteinase-9,MATRIX metalloproteinase-9 (EC 3.4.24.35) | protein | 158 | 25% helix, 17% strand | P14780 |
Ligands and binding sites
- B9Z · (2~{S})-2-[2-[4-(4-methoxyphenyl) phenyl]sulfanylphenyl]pentanedioic acid · ligand · chains A
- PZE · piperazine · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.58 | 0.86 | 22 | ZN, B9Z |
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 P14780
- Elsewhere: RCSB PDB 6ESM · PDBe 6ESM · UniProt P14780
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