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Crystal structure analysis of product bound methionine aminopeptidase type 1C from mycobacterium tuberculosis
Analyse Crystal structure analysis of product bound methionine aminopeptidase type 1C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YJ3
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase
- EC
- 3.4.11.18
- UniProt
- P0A5J2
- Ligands
- MET, CO, K
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase (EC 3.4.11.18) | protein | 282 | 24% helix, 24% strand | P0A5J2 |
Ligands and binding sites
- MET · Methionine · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · chains A
- K · Potassium ion · metal · chains A
- BME · Beta-mercaptoethanol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.55 | 0.81 | 27 | MET |
| 2 | 78 | 0.35 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 1YJ3 · Crystal structure analysis of product bound methionine aminopeptidase Type 1c from… · the same entry in another collection · 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 P0A5J2
- Elsewhere: RCSB PDB 1YJ3 · PDBe 1YJ3 · UniProt P0A5J2
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