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Crystal structure of abhpai-zn-pyruvate-4-hydroxybenzaldehyde complex, class II aldolase, hpai from acinetobacter baumannii
Analyse Crystal structure of abhpai-zn-pyruvate-4-hydroxybenzaldehyde complex, class II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ETI
- Type
- protein
- Length
- 759 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A5R9HKL3
- Ligands
- PYR, HBA, ZN, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 253 | — | A0A5R9HKL3 |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · 3 copies · chains A, B, C
- HBA · P-hydroxybenzaldehyde · ligand · 3 copies · chains A, B, C
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
- CA · Calcium ion · metal · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ETI · Crystal structure of AbHpaI-Zn-pyruvate-4-hydroxybenzaldehyde complex, Class II aldolase… · 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 A0A5R9HKL3
- Elsewhere: RCSB PDB 7ETI · PDBe 7ETI · UniProt A0A5R9HKL3
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