Research workbench
Crystal structure of human protein N-terminal glutamine amidohydrolase
Analyse Crystal structure of human protein N-terminal glutamine amidohydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W79
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein N-terminal glutamine amidohydrolase
- EC
- 3.5.1.-
- UniProt
- Q96HA8
- Ligands
- SO4, CO3
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein N-terminal glutamine amidohydrolase (EC 3.5.1.-) | protein | 202 | 27% helix, 21% strand | Q96HA8 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A
- CO3 · Carbonate ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4W79 · Crystal Structure of Human Protein N-terminal Glutamine Amidohydrolase · the same entry in another collection · chain A against A, TM-score 1.00
- Q96HA8 · AlphaFold monomer V2.0 prediction for protein N-terminal glutamine amidohydrolase (Q96HA8) · 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 Q96HA8
- Elsewhere: RCSB PDB 4W79 · PDBe 4W79 · UniProt Q96HA8
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