MolNFT v1 · #147766 · protein

Crystal structure a of the angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor.

6EN5 · Angiotensin-converting enzyme: “Crystal structure a of the angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor.”. X-ray diffraction, 8 ligands (BJ2, NAG, FUC), 20 pockets (best druggability 0.87). MolNFT v1…

PDB: 6EN5
Type: protein
Length: 2,433 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Angiotensin-converting enzyme
EC: 3.2.1.-, 3.4.15.1
UniProt: P12821
Ligands: BJ2, NAG, FUC, BMA, MAN, ZN, MG, CL
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 4 distinct chains · 62% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1)	protein	605	62% helix, 3% strand	P12821
B	Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1)	protein	608	62% helix, 2% strand	P12821
C	Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1)	protein	606	62% helix, 3% strand	P12821
D	Angiotensin-converting enzyme (EC 3.2.1.-, 3.4.15.1)	protein	614	62% helix, 3% strand	P12821

Ligands and binding sites

BJ2 · (2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid · ligand · 4 copies · chains A, B, C, D
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 24 copies · chains A, B, C, D
FUC · alpha-L-fucopyranose · sugar · 7 copies · chains A, B, C, D
BMA · beta-D-mannopyranose · sugar · 5 copies · chains A, B, C, D
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains D
ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
CL · Chloride ion · ion · 4 copies · chains A, B, C, D
EDO · 1,2-ethanediol · additive · 23 copies · chains A, B, C, D
PEG · Di(hydroxyethyl)ether · additive · 12 copies · chains A, B, C, D
ACT · Acetate ion · additive · 6 copies · chains A, B, C, D
PG4 · Tetraethylene glycol · additive · 2 copies · chains B, C
PE3 · 3,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diol · additive · chains A
PGE · Triethylene glycol · additive · chains A, B
XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · additive · chains C, D

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1079	0.87	0.88	112	BJ2, MG, PEG, EDO
2	1155	0.87	0.88	123	BJ2, MG, PEG
3	1138	0.87	0.88	116	BJ2, MG, PEG, EDO
4	582	0.86	0.91	67	BJ2, MG
5	282	0.78	0.90	31	EDO

Interfaces

3 interfaces between chains.

A–B · 1046 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 293 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 116 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide, 12 glycan (disulfide, N-glycosylation).

Compared structures

6EN5 · Crystal structure A of the Angiotensin-1 converting enzyme N-domain in complex with a… · the same entry in another collection · chain D against D, TM-score 1.00
P12821 · AlphaFold monomer V2.0 prediction for angiotensin-converting enzyme (P12821) · a predicted model of the same protein · chain C 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 P12821
Elsewhere: RCSB PDB 6EN5 · PDBe 6EN5 · UniProt P12821

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