Research workbench
Mycobacterium tuberculosis methionine aminopeptidase type 1C in complex with 2-hydroxyethyl disulfide
Analyse Mycobacterium tuberculosis methionine aminopeptidase type 1C in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IDY
- Type
- protein
- Length
- 282 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
- P0A5J2
- Ligands
- K
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2 (EC 3.4.11.18) | protein | 282 | 24% helix, 24% strand | P0A5J2 |
Ligands and binding sites
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 | 158 | 0.57 | 0.82 | 29 | HED |
| 2 | 102 | 0.40 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 4IDY · Mycobacterium Tuberculosis Methionine aminopeptidase Type 1c in complex with… · 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 4IDY · PDBe 4IDY · UniProt P0A5J2
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