Research workbench
Crystal structure of human methionine aminopeptidase (HSMETAP1B) in complex with kv-P2-4H-05
Analyse Crystal structure of human methionine aminopeptidase (HSMETAP1B) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LZC
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase 1
- EC
- 3.4.11.18
- UniProt
- P53582
- Ligands
- EYL, CO, NA, MG
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 1 (EC 3.4.11.18) | protein | 304 | 27% helix, 23% strand | P53582 |
Ligands and binding sites
- EYL · ~{N}-oxidanyl-1-(phenylmethyl)pyrrolo[2,3-b]pyridine-4-carboxamide · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.63 | 0.94 | 20 | empty |
| 2 | 266 | 0.55 | 0.77 | 33 | EYL, GOL |
Compared structures
- 6LZC · crystal structure of Human Methionine aminopeptidase (HsMetAP1b) in complex with… · 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 6LZC · PDBe 6LZC · UniProt P53582
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