Research workbench
Crystal structure of the S112A/H265Q mutant of a C-C hydrolase, bphd from burkholderia xenovorans LB400, after exposure to its substrate hopda
Analyse Crystal structure of the S112A/H265Q mutant of a C-C hydrolase, bphd from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V1M
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
- EC
- 3.7.1.8
- UniProt
- P47229
- Ligands
- HPK
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (EC 3.7.1.8) | protein | 283 | 47% helix, 19% strand | P47229 |
Ligands and binding sites
- HPK · (3E)-2,6-dioxo-6-phenylhex-3-enoate · ligand · chains A
- MLI · Malonate ion · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.71 | 0.86 | 37 | HPK |
| 2 | 128 | 0.53 | 0.81 | 23 | empty |
Compared structures
- 3V1M · Crystal Structure of the S112A/H265Q mutant of a C-C hydrolase, BphD from Burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00
- P47229 · AlphaFold monomer V2.0 prediction for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase… · 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 P47229
- Elsewhere: RCSB PDB 3V1M · PDBe 3V1M · UniProt P47229
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