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Structure of human aldosterone synthase, CYP11B2, in complex with fadrozole

Analyse Structure of human aldosterone synthase, CYP11B2, in complex with fadrozole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FDH
Type: protein
Length: 5,568 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 11B2, mitochondrial
EC: 1.14.15.4, 1.14.15.5
UniProt: P19099
Ligands: HEM, 0T3
Pockets: 20 · best druggability 0.88

Structure

x-ray diffraction · 7 distinct chains · 57% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, G	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	463	58% helix, 10% strand	P19099
B, D	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	465	57% helix, 11% strand	P19099
C, H, I, J	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	462	57% helix, 10% strand	P19099
E	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	470	57% helix, 10% strand	P19099
F	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	469	57% helix, 9% strand	P19099
K	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	469	56% helix, 10% strand	P19099
L	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	456	57% helix, 10% strand	P19099

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
0T3 · 4-[(5R)-5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl]benzonitrile · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	902	0.88	0.89	101	HEM, 0T3
2	826	0.87	0.89	88	HEM, 0T3
3	858	0.87	0.89	89	HEM, 0T3
4	917	0.87	0.88	92	HEM, 0T3
5	805	0.87	0.89	85	HEM, 0T3

Interfaces

22 interfaces between chains.

H–I · 768 Å² buried · 12 hydrogen bonds · protein-protein
B–F · 761 Å² buried · 15 hydrogen bonds · protein-protein
C–E · 758 Å² buried · 17 hydrogen bonds · protein-protein
B–D · 758 Å² buried · 14 hydrogen bonds · protein-protein
G–L · 753 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4FDH · Structure of human aldosterone synthase, CYP11B2, in complex with fadrozole · the same entry in another collection · chain L against L, 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 P19099
Elsewhere: RCSB PDB 4FDH · PDBe 4FDH · UniProt P19099

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