MolNFT v1 · #46653 · protein
Human methionine aminopeptidase-2 complexed with sb-587094
2OAZ · Human methionine amino peptidase 2: “Human methionine aminopeptidase-2 complexed with sb-587094”. X-ray diffraction, 2 ligands (I96, CO), 3 pockets (best druggability 0.69). MolNFT v1 #46653 on GenesisL1: 3D structure, binding sites…
- PDB
- 2OAZ
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human methionine amino peptidase 2
- EC
- 3.4.11.18
- UniProt
- P50579
- Ligands
- I96, CO
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human methionine amino peptidase 2 (EC 3.4.11.18) | protein | 355 | 29% helix, 26% strand | P50579 |
Ligands and binding sites
- I96 · N-(2-isopropylphenyl)-3-[(2-thienylmethyl)thio]-1H-1,2,4-triazol-5-amine · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.69 | 0.85 | 40 | I96 |
| 2 | 54 | 0.43 | 0.83 | 15 | empty |
| 3 | 53 | 0.25 | 0.72 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P50579
- Elsewhere: RCSB PDB 2OAZ · PDBe 2OAZ · UniProt P50579
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