Research workbench
Histidine-containing phosphotransfer domain of arcb from escherichia COLI
Analyse Histidine-containing phosphotransfer domain of arcb from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A0B
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hpt domain
- EC
- 2.7.3.-
- UniProt
- P22763
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hpt domain (EC 2.7.3.-) | protein | 118 | 84% helix, 0% strand | P22763 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2A0B · Histidine-containing phosphotransfer domain of arcb from escherichia COLI · 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 P22763
- Elsewhere: RCSB PDB 2A0B · PDBe 2A0B · UniProt P22763
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