Research workbench
Crystal structure analysis of N-acetylneuraminate lyase from haemophilus influenzae: crystal form III
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
- 1F6P
- Type
- protein
- Length
- 1,172 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyl neuraminate lyase
- EC
- 4.1.3.3
- UniProt
- P44539
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | N-acetyl neuraminate lyase (EC 4.1.3.3) | protein | 293 | 52% helix, 14% strand | P44539 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.72 | 0.90 | 31 | empty |
| 2 | 182 | 0.70 | 0.88 | 31 | empty |
| 3 | 394 | 0.68 | 0.80 | 44 | empty |
| 4 | 348 | 0.68 | 0.81 | 37 | empty |
| 5 | 339 | 0.68 | 0.81 | 36 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1466 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1463 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1116 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1113 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1F6P · 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 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 P44539
- Elsewhere: RCSB PDB 1F6P · PDBe 1F6P · UniProt P44539
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