MolNFT v1 · #166956 · protein
Crystal structure of histidine ammonia-lyase from trypanosoma cruzi
6V6H: “Crystal structure of histidine ammonia-lyase from trypanosoma cruzi”. X-ray diffraction, 18 pockets (best druggability 0.74). MolNFT v1 #166956 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6V6H
- Type
- protein
- Length
- 2,027 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine ammonia-lyase
- EC
- 4.3.1.3
- UniProt
- Q4E133
- Pockets
- 18 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 60% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine ammonia-lyase (EC 4.3.1.3) | protein | 509 | 60% helix, 6% strand | Q4E133 |
| B | Histidine ammonia-lyase (EC 4.3.1.3) | protein | 504 | 60% helix, 6% strand | Q4E133 |
| C | Histidine ammonia-lyase (EC 4.3.1.3) | protein | 509 | 60% helix, 6% strand | Q4E133 |
| D | Histidine ammonia-lyase (EC 4.3.1.3) | protein | 505 | 60% helix, 6% strand | Q4E133 |
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.74 | 0.97 | 32 | empty |
| 2 | 490 | 0.74 | 0.82 | 55 | empty |
| 3 | 553 | 0.73 | 0.81 | 58 | empty |
| 4 | 526 | 0.71 | 0.80 | 62 | empty |
| 5 | 428 | 0.70 | 0.81 | 57 | empty |
Interfaces
6 interfaces between chains.
- A–B · 4118 Ų buried · 74 hydrogen bonds · protein-protein
- C–D · 4076 Ų buried · 73 hydrogen bonds · protein-protein
- A–C · 2841 Ų buried · 35 hydrogen bonds · protein-protein
- B–D · 2822 Ų buried · 35 hydrogen bonds · protein-protein
- B–C · 171 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 modified (nonstandard, oxidation).
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 Q4E133
- Elsewhere: RCSB PDB 6V6H · PDBe 6V6H · UniProt Q4E133
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