MolNFT v1 · #1588 · protein
Human methionine aminopeptidase 2 complexed with tnp-470
1B6A: “Human methionine aminopeptidase 2 complexed with tnp-470”. X-ray diffraction, 2 ligands (TN4, CO), 3 pockets (best druggability 0.69). MolNFT v1 #1588 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1B6A
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase
- EC
- 3.4.11.18
- UniProt
- P50579
- Ligands
- TN4, CO
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase (EC 3.4.11.18) | protein | 355 | 32% helix, 27% strand | P50579 |
Ligands and binding sites
- TN4 · (1R,2S,3S,4R)-4-hydroxy-2-methoxy-4-methyl-3-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]cyclohexyl (chloroacetyl)carbamate · 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 | 284 | 0.69 | 0.84 | 40 | TN4 |
| 2 | 73 | 0.49 | 0.84 | 16 | empty |
| 3 | 63 | 0.28 | 0.73 | 12 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 1B6A · PDBe 1B6A · UniProt P50579
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