Research workbench
Hydrogenase maturation protein hypf "acylphosphatase-like" N-terminal domain (hypf-acp) in complex with sulfate
Analyse Hydrogenase maturation protein hypf "acylphosphatase-like" N-terminal domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GXT
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrogenase maturation protein hypf
- UniProt
- P30131
- Ligands
- CL, SO4
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydrogenase maturation protein hypf | protein | 88 | 24% helix, 41% strand | P30131 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1GXT · Hydrogenase Maturation Protein HypF "acylphosphatase-like" N-terminal domain (HypF-ACP)… · the same entry in another collection · chain A against A, TM-score 1.00
- P30131 · AlphaFold monomer V2.0 prediction for carbamoyltransferase hypf (P30131) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P30131
- Elsewhere: RCSB PDB 1GXT · PDBe 1GXT · UniProt P30131
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