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Crystal structure of Cytochrome C Peroxidase W191G-Gateless in complex with 4-Azaindole

Analyse Crystal structure of Cytochrome C Peroxidase W191G-Gateless in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JPL
Type: protein
Length: 289 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.41
Source: Saccharomyces cerevisiae
Molecule: Cytochrome c peroxidase
EC: 1.11.1.5
UniProt: B3LRE1
Ligands: HEM, 4JP, PO4
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.41 · 1 distinct chain · 51% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome c peroxidase (EC 1.11.1.5)	protein	289	51% helix, 7% strand	B3LRE1

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
4JP · 1H-pyrrolo[3,2-b]pyridine · ligand · chains A
PO4 · Phosphate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.82	0.90	57	HEM, 4JP
2	110	0.41	0.76	23	PO4

Compared structures

4JPL · Crystal structure of cytochrome C peroxidase W191G-gateless in complex with 4-azaindole · the same entry in another collection · 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 B3LRE1
Elsewhere: RCSB PDB 4JPL · PDBe 4JPL · UniProt B3LRE1

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