MolNFT v1 · #13442 · protein

The crystal structure of saccharomyces cerevisiae ferrochelatase

1LBQ: “The crystal structure of saccharomyces cerevisiae ferrochelatase”. X-ray diffraction, 9 pockets (best druggability 0.82). MolNFT v1 #13442 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LBQ
Type: protein
Length: 710 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferrochelatase
EC: 4.99.1.1
UniProt: P16622
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferrochelatase (EC 4.99.1.1)	protein	356	48% helix, 14% strand	P16622
B	Ferrochelatase (EC 4.99.1.1)	protein	354	47% helix, 14% strand	P16622

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	161	0.82	0.98	39	empty
2	408	0.81	0.89	57	empty
3	722	0.77	0.82	56	empty
4	304	0.60	0.79	28	empty
5	326	0.58	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 1470 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1LBQ · The crystal structure of Saccharomyces cerevisiae 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 B 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 P16622
Elsewhere: RCSB PDB 1LBQ · PDBe 1LBQ · UniProt P16622

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