MolNFT v1 · #115490 · protein
Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) mutant H59N from the acidophilic bacterium acetobacter aceti, at pH 5.4
5CLG: “Structure of pure (N5-carboxyaminoimidazole ribonucleotide mutase) mutant H59N from the acidophilic bacterium…”. X-ray diffraction. MolNFT v1 #115490 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CLG
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N5-carboxyaminoimidazole ribonucleotide mutase
- EC
- 5.4.99.18
- UniProt
- A0A063X4U8
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N5-carboxyaminoimidazole ribonucleotide mutase (EC 5.4.99.18) | protein | 156 | 48% helix, 15% strand | A0A063X4U8 |
| B | N5-carboxyaminoimidazole ribonucleotide mutase (EC 5.4.99.18) | protein | 160 | 47% helix, 16% strand | A0A063X4U8 |
Ligands and binding sites
- CIT · Citric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1697 Ų buried · 31 hydrogen bonds · protein-protein
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 A0A063X4U8
- Elsewhere: RCSB PDB 5CLG · PDBe 5CLG · UniProt A0A063X4U8
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