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Structure and atypical hydrolysis mechanism of the nudix hydrolase ORF153 (ymfb) from escherichia COLI
Analyse Structure and atypical hydrolysis mechanism of the nudix hydrolase ORF153… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NFW
- Type
- protein
- Length
- 1,784 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G7RNP0
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, G, H, K | — | protein | 150 | — | G7RNP0 |
| F | — | protein | 153 | — | G7RNP0 |
| I | — | protein | 138 | — | G7RNP0 |
| J | — | protein | 152 | — | G7RNP0 |
| L | — | protein | 141 | — | G7RNP0 |
Compared structures
- 4NFW · Structure and atypical hydrolysis mechanism of the Nudix hydrolase Orf153 (YmfB) from… · 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 G7RNP0
- Elsewhere: RCSB PDB 4NFW · PDBe 4NFW · UniProt G7RNP0
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