MolNFT v1 · #3479 · protein

Crystal structure of chloroplast cytochrome F reveals a novel cytochrome fold and unexpected heme ligation

1CTM: “Crystal structure of chloroplast cytochrome F reveals a novel cytochrome fold and unexpected heme ligation”. X-ray diffraction, 1 ligand (HEC), 1 pocket (best druggability 0.71). MolNFT v1 #3479 on GenesisL1: 3D structure, binding…

PDB: 1CTM
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome F
UniProt: P36438
Ligands: HEC
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome F	protein	250	11% helix, 40% strand	P36438

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	181	0.71	0.89	33	HEC

Modifications

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

Compared structures

1CTM · Crystal structure of chloroplast cytochrome F reveals a novel cytochrome fold and… · the same entry in another collection · chain A against A, TM-score 1.00
P36438 · AlphaFold monomer V2.0 prediction for cytochrome F (P36438) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P36438
Elsewhere: RCSB PDB 1CTM · PDBe 1CTM · UniProt P36438

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