Research workbench
Crystal structure of GTP cyclohydrolase I from yersinia pestis complexed with GTP
Analyse Crystal structure of GTP cyclohydrolase I from yersinia pestis complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DU6
- Type
- protein
- Length
- 1,084 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q66C86
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 219 | — | Q66C86 |
| B, D | — | protein | 216 | — | Q66C86 |
| E | — | protein | 214 | — | Q66C86 |
Compared structures
- 4DU6 · Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP · the same entry in another collection · chain A against A, TM-score 1.00
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 Q66C86
- Elsewhere: RCSB PDB 4DU6 · PDBe 4DU6 · UniProt Q66C86
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