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Crystal structure of ferrochelatase hemh-1 from bacillus anthracis, str. ames

Analyse Crystal structure of ferrochelatase hemh-1 from bacillus anthracis, str. ames in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C8J
Type: protein
Length: 621 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferrochelatase 1
EC: 4.99.1.1
UniProt: Q81U22
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferrochelatase 1 (EC 4.99.1.1)	protein	311	50% helix, 17% strand	Q81U22
B	Ferrochelatase 1 (EC 4.99.1.1)	protein	310	49% helix, 17% strand	Q81U22

Pockets

3 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	1094	0.79	0.81	89	empty
2	599	0.77	0.83	58	empty
3	93	0.43	0.79	26	empty

Interfaces

1 interface between chains.

A–B · 404 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2C8J · CRYSTAL STRUCTURE OF ferrochelatase HemH-1 from Bacillus anthracis, str. Ames · the same entry in another collection · chain A against A, TM-score 1.00
Q81U22 · AlphaFold monomer V2.0 prediction for coproporphyrin III ferrochelatase 1 (Q81U22) · a predicted model of the same protein · chain B against A, TM-score 0.99

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Every structure of UniProt Q81U22
Elsewhere: RCSB PDB 2C8J · PDBe 2C8J · UniProt Q81U22

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