MolNFT v1 · #12731 · protein
Human methionine aminopeptidase type II in complex with D- methionine
1KQ0 · Methionine aminopeptidase 2: “Human methionine aminopeptidase type II in complex with D- methionine”. X-ray diffraction, 2 ligands (MED, ZN), 3 pockets (best druggability 0.66). MolNFT v1 #12731 on GenesisL1: 3D structure, binding…
- PDB
- 1KQ0
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase 2
- EC
- 3.4.11.18
- UniProt
- P50579
- Ligands
- MED, ZN
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2 (EC 3.4.11.18) | protein | 354 | 30% helix, 27% strand | P50579 |
Ligands and binding sites
- MED · D-methionine · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- TBU · Tertiary-butyl alcohol · additive · 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 | 197 | 0.66 | 0.85 | 35 | MED |
| 2 | 62 | 0.48 | 0.85 | 16 | empty |
| 3 | 51 | 0.24 | 0.72 | 11 | TBU |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1KQ0 · Human methionine aminopeptidase type II in complex with D-methionine · the same entry in another collection · chain A against A, TM-score 1.00
- P50579 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 2 (P50579) · 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 P50579
- Elsewhere: RCSB PDB 1KQ0 · PDBe 1KQ0 · UniProt P50579
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