MolNFT v1 · #140749 · protein
Human methionine aminopeptidase type 1B (F309M mutant) in complex with ovalicin
5YKP: “Human methionine aminopeptidase type 1B (F309M mutant) in complex with ovalicin”. X-ray diffraction, 3 ligands (OVA, CO, K). MolNFT v1 #140749 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5YKP
- Type
- protein
- Length
- 305 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53582
- Ligands
- OVA, CO, K
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 305 | — | P53582 |
Ligands and binding sites
- OVA · 3,4-dihydroxy-2-methoxy-4-methyl-3-[2-methyl-3-(3-methyl-but-2-enyl) -oxiranyl]-cyclohexanone · ligand · chains A
- CO · Cobalt (II) ion · metal · 3 copies · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YKP · Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin · the same entry in another collection · chain A against A, TM-score 1.00
- P53582 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 1 (P53582) · a predicted model of the same protein · 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 P53582
- Elsewhere: RCSB PDB 5YKP · PDBe 5YKP · UniProt P53582
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.