Research workbench
Human catalytic mmp-12 in complex with 5-(1,2-dithiolan-3-yl)-N-(3- HYDROXYPROPYL)PENTANAMIDE
Analyse Human catalytic mmp-12 in complex with 5-(1,2-dithiolan-3-yl)-N-(3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N5K
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39900
- Ligands
- HAE, 8NW, CA, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 156 | — | P39900 |
Ligands and binding sites
- HAE · Acetohydroxamic acid · ligand · chains A
- 8NW · 5-[(3~{S})-1,2-dithiolan-3-yl]-~{N}-(3-oxidanylpropyl) pentanamide · 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.
Compared structures
- 5N5K · Human catalytic MMP-12 in complex with 5-(1,2-dithiolan-3-yl)-N-(3-hydroxypropyl)pentanami… · 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 5N5K · PDBe 5N5K · UniProt P39900
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.