Research workbench

Human oxytocin receptor (otr) oxytocin gq chimera (mgoqi) complex

Analyse Human oxytocin receptor (otr) oxytocin gq chimera (mgoqi) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QVM
Type: protein
Length: 1,094 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanine nucleotide-binding protein G(O) subunit ALPHA,CDNA FLJ31446 fis, clone…
UniProt: A0A1W2PS82, B3KP89, P09471, P62873, P59768, P01178, P30559
Ligands: NH2
Pockets: 12 · best druggability 0.82

Structure

electron microscopy · 6 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanine nucleotide-binding protein G(O) subunit ALPHA,CDNA FLJ31446 fis, clone NT2NE2000909, highly similar to guanine nucleotide-binding protein G(O) subunit alpha 1	protein	210	43% helix, 17% strand	A0A1W2PS82, B3KP89, P09471
B	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	protein	338	8% helix, 40% strand	P62873
G	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	protein	56	55% helix, 0% strand	P59768
L	Oxytocin	protein	9	0% helix, 0% strand	P01178
R	Oxytocin receptor	protein	250	82% helix, 2% strand	P30559
S	Antibody fragment SCFV16	protein	231	4% helix, 48% strand	—

Ligands and binding sites

NH2 · Amino group · ion · chains L, R

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	782	0.82	0.85	66	empty
2	392	0.56	0.75	50	empty
3	101	0.51	0.82	22	empty
4	112	0.51	0.82	23	empty
5	193	0.50	0.77	21	empty

Interfaces

6 interfaces between chains.

B–G · 2169 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1262 Å² buried · 11 hydrogen bonds · protein-protein
L–R · 822 Å² buried · 8 hydrogen bonds · protein-protein
A–R · 723 Å² buried · 7 hydrogen bonds · protein-protein
A–S · 583 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

7QVM · Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex · the same entry in another collection · chain S against S, TM-score 1.00
P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain B against A, TM-score 0.99
P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain G against A, TM-score 0.92
P30559 · AlphaFold monomer V2.0 prediction for oxytocin receptor (P30559) · a predicted model of the same protein · chain R against A, TM-score 0.89
P09471 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(O) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.76
P01178 · AlphaFold monomer V2.0 prediction for oxytocin-neurophysin 1 (P01178) · a predicted model of the same protein · chain L against A, TM-score 0.27

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 A0A1W2PS82
Every structure of UniProt B3KP89
Every structure of UniProt P09471
Every structure of UniProt P62873
Every structure of UniProt P59768
Every structure of UniProt P01178
Every structure of UniProt P30559
Elsewhere: RCSB PDB 7QVM · PDBe 7QVM · UniProt A0A1W2PS82 · UniProt B3KP89 · UniProt P09471 · UniProt P62873 · UniProt P59768 · UniProt P01178 · UniProt P30559

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