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Solution structure of methylophilus methylotrophus cytochrome C''. insights into the structural basis of haem-ligand detachment

Analyse Solution structure of methylophilus methylotrophus cytochrome C''. insights… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E8E
Type: protein
Length: 124 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C''
UniProt: Q9RQB9
Ligands: HEC
Pockets: 1 · best druggability 0.64

Structure

solution nmr · 1 distinct chain · 35% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C''	protein	124	35% helix, 6% strand	Q9RQB9

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	304	0.64	0.80	42	HEC

Modifications

Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).

Compared structures

1E8E · Solution Structure of Methylophilus methylotrophus Cytochrome c''. Insights into the… · the same entry in another collection · chain A against A, TM-score 1.00
Q9RQB9 · AlphaFold monomer V2.0 prediction for cytochrome C'' (Q9RQB9) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q9RQB9
Elsewhere: RCSB PDB 1E8E · PDBe 1E8E · UniProt Q9RQB9

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