Research workbench
Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome C peroxidase
Analyse Effect of unnatural heme substitution on kinetics of electron transfer in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BEP
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yeast cytochrome C peroxidase
- EC
- 1.11.1.5
- UniProt
- P00431
- Ligands
- CCH
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Yeast cytochrome C peroxidase (EC 1.11.1.5) | protein | 291 | 51% helix, 8% strand | P00431 |
Ligands and binding sites
- CCH · [7-ethenyl-12-formyl-3,8,13,17-tertramethyl-21H,23H-porphine-2,18-dipropanoato(2)-n21,n22,n23,n24]iron · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.81 | 0.90 | 46 | CCH |
| 2 | 78 | 0.40 | 0.78 | 16 | empty |
Compared structures
- 1BEP · Effect of unnatural heme substitution on kinetics of electron transfer in cytochrome C… · the same entry in another collection · chain A against A, TM-score 1.00
- P00431 · AlphaFold monomer V2.0 prediction for cytochrome C peroxidase, mitochondrial (P00431) · 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 P00431
- Elsewhere: RCSB PDB 1BEP · PDBe 1BEP · UniProt P00431
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