MolNFT v1 · #180029 · protein
AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3)
P0A6Z3: “AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3)”. MolNFT v1 #180029 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P0A6Z3
- Type
- protein
- Length
- 624 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- UniProt
- P0A6Z3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 624 | — | P0A6Z3 |
Compared structures
- 2IOQ · Crystal Structure of full-length HTPG, the Escherichia coli HSP90 · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 2IOQ · Crystal structure of full-length htpg, the escherichia COLI HSP90 · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 1Y4S · Conformation rearrangement of heat shock protein 90 upon ADP binding · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 1Y4S · Conformation rearrangement of heat shock protein 90 upon ADP binding · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 1Y4U · Conformation rearrangement of heat shock protein 90 upon ADP binding · an experimental structure of the same protein · chain A against A, TM-score 0.71
- 1Y4U · Conformation rearrangement of heat shock protein 90 upon ADP binding · an experimental structure of the same protein · chain A against A, TM-score 0.71
- 2IOP · Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP · an experimental structure of the same protein · chain A against B, TM-score 0.61
- 2IOP · Crystal structure of full-length htpg, the escherichia COLI HSP90, bound to ADP · an experimental structure of the same protein · chain A against B, TM-score 0.61
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: UniProt P0A6Z3 · AlphaFold DB P0A6Z3
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