MolNFT v1 · #10379 · protein
Structure of catalase hpii from escherichia COLI
1IPH: “Structure of catalase hpii from escherichia COLI”. X-ray diffraction, 1 ligand (HEM), 20 pockets (best druggability 0.89). MolNFT v1 #10379 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1IPH
- Type
- protein
- Length
- 2,908 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catalase hpii
- EC
- 1.11.1.6
- UniProt
- P21179
- Ligands
- HEM
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Catalase hpii (EC 1.11.1.6) | protein | 727 | 32% helix, 18% strand | P21179 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, 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, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.89 | 0.95 | 59 | empty |
| 2 | 624 | 0.89 | 0.95 | 56 | empty |
| 3 | 1182 | 0.88 | 0.89 | 158 | empty |
| 4 | 1161 | 0.88 | 0.89 | 144 | empty |
| 5 | 371 | 0.87 | 0.95 | 57 | HEM |
Interfaces
6 interfaces between chains.
- A–B · 6155 Ų buried · 108 hydrogen bonds · protein-protein
- C–D · 6155 Ų buried · 108 hydrogen bonds · protein-protein
- B–D · 5924 Ų buried · 88 hydrogen bonds · protein-protein
- A–C · 5924 Ų buried · 86 hydrogen bonds · protein-protein
- A–D · 2247 Ų buried · 40 hydrogen bonds · protein-protein
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 P21179
- Elsewhere: RCSB PDB 1IPH · PDBe 1IPH · UniProt P21179
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