Research workbench
Structural and functional study of succinyl-ornithine transaminase from E. COLI
Analyse Structural and functional study of succinyl-ornithine transaminase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ADE
- Type
- protein
- Length
- 750 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Succinylornithine transaminase
- EC
- 2.6.1.17, 2.6.1.81
- UniProt
- P77581
- Pockets
- 10 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinylornithine transaminase (EC 2.6.1.17, 2.6.1.81) | protein | 400 | 43% helix, 19% strand | P77581 |
| B | Succinylornithine transaminase (EC 2.6.1.17, 2.6.1.81) | protein | 350 | 42% helix, 21% strand | P77581 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.60 | 0.75 | 55 | empty |
| 2 | 201 | 0.52 | 0.77 | 26 | empty |
| 3 | 84 | 0.42 | 0.79 | 26 | empty |
| 4 | 103 | 0.40 | 0.76 | 14 | empty |
| 5 | 88 | 0.36 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 243 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4ADE · Structural and functional study of succinyl-ornithine transaminase from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P77581 · AlphaFold monomer V2.0 prediction for succinylornithine transaminase (P77581) · 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 P77581
- Elsewhere: RCSB PDB 4ADE · PDBe 4ADE · UniProt P77581
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