MolNFT v1 · #180665 · protein

H235C variant of yeast ferrochelatase

7L78 · Ferrochelatase, mitochondrial: “H235C variant of yeast ferrochelatase”. X-ray diffraction, 1 ligand (CHD), 9 pockets (best druggability 0.82). MolNFT v1 #180665 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7L78
Type: protein
Length: 711 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferrochelatase, mitochondrial
EC: 4.99.1.1
UniProt: P16622
Ligands: CHD
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferrochelatase, mitochondrial (EC 4.99.1.1)	protein	356	49% helix, 14% strand	P16622
B	Ferrochelatase, mitochondrial (EC 4.99.1.1)	protein	355	50% helix, 14% strand	P16622

Ligands and binding sites

CHD · Cholic acid · ligand · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.82	0.98	39	empty
2	809	0.79	0.82	60	empty
3	683	0.75	0.81	55	CHD
4	287	0.59	0.78	28	empty
5	277	0.54	0.76	24	empty

Interfaces

1 interface between chains.

A–B · 1519 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7L78 · H235C variant of Yeast Ferrochelatase · the same entry in another collection · chain A against A, TM-score 1.00
P16622 · AlphaFold monomer V2.0 prediction for ferrochelatase, mitochondrial (P16622) · a predicted model of the same protein · 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 P16622
Elsewhere: RCSB PDB 7L78 · PDBe 7L78 · UniProt P16622

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