Research workbench
Crystal structure analysis of N-acetylneuraminate lyase from haemophilus influenzae: crystal form II complexed with 4-deoxy-sialic acid
Analyse Crystal structure analysis of N-acetylneuraminate lyase from haemophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F74
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P44539
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 293 | — | P44539 |
Compared structures
- 1F74 · Crystal structure analysis of N-acetylneuraminate lyase from haemophilus influenzae… · the same entry in another collection · chain A against A, TM-score 1.00
- P44539 · AlphaFold monomer V2.0 prediction for N-acetylneuraminate lyase (P44539) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P44539
- Elsewhere: RCSB PDB 1F74 · PDBe 1F74 · UniProt P44539
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