Research workbench
Crystal structure of the N-terminal domain of htpg, the escherichia COLI HSP90, bound to ADP
Analyse Crystal structure of the N-terminal domain of htpg, the escherichia COLI HSP90… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IOR
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6Z3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 212 | — | P0A6Z3 |
Compared structures
- 2IOR · Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6Z3 · AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P0A6Z3
- Elsewhere: RCSB PDB 2IOR · PDBe 2IOR · UniProt P0A6Z3
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