MolNFT v1 · #22811 · protein
Crystal structure of NADPH depleted bovine liver catalase complexed with azide
1TH2: “Crystal structure of NADPH depleted bovine liver catalase complexed with azide”. X-ray diffraction, 2 ligands (HEM, AZI), 20 pockets (best druggability 0.88). MolNFT v1 #22811 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1TH2
- Type
- protein
- Length
- 1,996 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catalase
- EC
- 1.11.1.6
- UniProt
- P00432
- Ligands
- HEM, AZI
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Catalase (EC 1.11.1.6) | protein | 499 | 34% helix, 19% strand | P00432 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, D, B, C
- AZI · Azide ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.88 | 0.96 | 54 | empty |
| 2 | 433 | 0.88 | 0.96 | 54 | empty |
| 3 | 657 | 0.88 | 0.92 | 51 | empty |
| 4 | 1071 | 0.87 | 0.87 | 115 | AZI, HEM |
| 5 | 341 | 0.86 | 0.95 | 50 | HEM |
Interfaces
6 interfaces between chains.
- A–D · 4862 Ų buried · 77 hydrogen bonds · protein-protein
- B–C · 4851 Ų buried · 82 hydrogen bonds · protein-protein
- A–C · 4787 Ų buried · 62 hydrogen bonds · protein-protein
- B–D · 4662 Ų buried · 61 hydrogen bonds · protein-protein
- A–B · 2173 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (heme attachment).
Compared structures
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 P00432
- Elsewhere: RCSB PDB 1TH2 · PDBe 1TH2 · UniProt P00432
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