Research workbench
Pseudomonas aeruginosa metap, in mn form
Analyse Pseudomonas aeruginosa metap, in mn form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FO7
- Type
- protein
- Length
- 1,034 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase
- EC
- 3.4.11.18
- UniProt
- Q9HXY1
- Ligands
- MN
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Methionine aminopeptidase (EC 3.4.11.18) | protein | 258 | 29% helix, 27% strand | Q9HXY1 |
| B | Methionine aminopeptidase (EC 3.4.11.18) | protein | 260 | 28% helix, 27% strand | Q9HXY1 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 14 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 718 | 0.72 | 0.78 | 53 | empty |
| 2 | 603 | 0.68 | 0.77 | 55 | empty |
| 3 | 230 | 0.64 | 0.82 | 25 | MN |
| 4 | 231 | 0.63 | 0.82 | 24 | MN |
| 5 | 236 | 0.62 | 0.82 | 31 | empty |
Interfaces
4 interfaces between chains.
- B–D · 709 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 320 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 252 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 63 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4FO7 · Pseudomonas aeruginosa MetAP, in Mn form · 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 Q9HXY1
- Elsewhere: RCSB PDB 4FO7 · PDBe 4FO7 · UniProt Q9HXY1
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