MolNFT v1 · #134596 · protein

Cytochrome C - calixarene free

5T8W · CYC1P: “Cytochrome C - calixarene free”. X-ray diffraction, 2 ligands (HEC, CL), 5 pockets (best druggability 0.73). MolNFT v1 #134596 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5T8W
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CYC1P
UniProt: A0A0C6AZG8
Ligands: HEC, CL
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CYC1P	protein	108	41% helix, 2% strand	A0A0C6AZG8

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	194	0.73	0.89	31	HEC
2	182	0.73	0.89	34	HEC
3	122	0.44	0.77	19	empty
4	112	0.44	0.78	21	empty
5	73	0.34	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 516 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

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 A0A0C6AZG8
Elsewhere: RCSB PDB 5T8W · PDBe 5T8W · UniProt A0A0C6AZG8

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