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Structure of aldosterone synthase (CYP11B2) in complex with (+)-(R)-N- (4-(4-chloro-3-fluorophenyl)-5,6,7,8-tetrahydroisoquinolin-8-yl) propionamide

Analyse Structure of aldosterone synthase (CYP11B2) in complex with (+)-(R)-N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZGX
Type: protein
Length: 5,557 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, QHC
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, B, C, D, G, H	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	465	58% helix, 10% strand	P19099
E	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	459	57% helix, 10% strand	P19099
F	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	464	57% helix, 10% strand	P19099
I	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	458	57% helix, 10% strand	P19099
J	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	463	55% helix, 11% strand	P19099
K	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	461	56% helix, 10% strand	P19099
L	Cytochrome P450 11B2, mitochondrial (EC 1.14.15.4, 1.14.15.5)	protein	462	56% 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
QHC · N-[(8R)-4-(4-chloro-3-fluorophenyl)-5,6,7,8-tetrahydroisoquinolin-8-yl]propanamide · ligand · 10 copies · chains A, B, C, D, E, F, 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	988	0.88	0.89	99	HEM, QHC
2	852	0.87	0.89	82	HEM
3	932	0.87	0.88	84	HEM, QHC
4	658	0.87	0.91	59	HEM, QHC
5	931	0.86	0.88	90	HEM, QHC

Interfaces

24 interfaces between chains.

H–J · 763 Å² buried · 14 hydrogen bonds · protein-protein
G–I · 759 Å² buried · 13 hydrogen bonds · protein-protein
E–F · 753 Å² buried · 13 hydrogen bonds · protein-protein
B–G · 749 Å² buried · 17 hydrogen bonds · protein-protein
C–H · 744 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

P19099 · AlphaFold monomer V2.0 prediction for cytochrome P450 11B2, mitochondrial (P19099) · a predicted model of the same protein · chain I 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 P19099
Elsewhere: RCSB PDB 4ZGX · PDBe 4ZGX · UniProt P19099

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