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Crystallization and X-ray structure determination of cytochrome C2 from rhodobacter sphaeroides in three crystal forms

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PDB: 1CXC
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C2
UniProt: P00095
Ligands: HEC
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C2	protein	124	43% helix, 6% strand	P00095

Ligands and binding sites

HEC · Heme C · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	218	0.76	0.90	36	HEC

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

1CXC · Crystallization and X-ray structure determination of cytochrome C2 from rhodobacter… · 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 P00095
Elsewhere: RCSB PDB 1CXC · PDBe 1CXC · UniProt P00095

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