Research workbench
Crystal structure of mutant R322A of beta-alanine synthase from saccharomyces kluyveri
Analyse Crystal structure of mutant R322A of beta-alanine synthase from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V8V
- Type
- protein
- Length
- 1,732 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-alanine synthase
- EC
- 3.5.1.6
- UniProt
- Q96W94
- Ligands
- URP, ZN
- Pockets
- 14 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-alanine synthase (EC 3.5.1.6) | protein | 435 | 36% helix, 23% strand | Q96W94 |
| B, C | Beta-alanine synthase (EC 3.5.1.6) | protein | 431 | 36% helix, 24% strand | Q96W94 |
| D | Beta-alanine synthase (EC 3.5.1.6) | protein | 435 | 35% helix, 23% strand | Q96W94 |
Ligands and binding sites
- URP · N-(aminocarbonyl)-beta-alanine · ligand · 3 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.77 | 0.79 | 103 | empty |
| 2 | 486 | 0.73 | 0.82 | 63 | empty |
| 3 | 515 | 0.66 | 0.77 | 62 | URP |
| 4 | 437 | 0.64 | 0.78 | 61 | DTT, URP |
| 5 | 438 | 0.63 | 0.77 | 53 | ZN, URP |
Interfaces
5 interfaces between chains.
- C–D · 2254 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 2252 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 1092 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 65 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 64 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 2V8V · Crystal structure of mutant R322A of beta-alanine synthase from Saccharomyces kluyveri · 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 Q96W94
- Elsewhere: RCSB PDB 2V8V · PDBe 2V8V · UniProt Q96W94
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