7MBY
Human Cholecystokinin 1 receptor (CCK1R) Gq chimera (mGsqi) complex
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | polymer | 340 | 37416.9 | 1 | UniProt (P54311) Pfam (PF00400) In PDB | Rattus norvegicus (Rat) | Transducin beta chain 1 |
2 | G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | polymer | 71 | 7861.1 | 1 | UniProt (P59768) Pfam (PF00631) In PDB | Homo sapiens (Human) | G gamma-I |
3 | P | Cholecystokinin-8 | polymer | 9 | 1142.3 | 1 | UniProt (P06307) In PDB | Homo sapiens | CCK-8 |
4 | R | Cholecystokinin receptor type A | polymer | 427 | 47754.9 | 1 | UniProt (P32238) Pfam (PF09193) Pfam (PF00001) In PDB | Homo sapiens (Human) | CCK-A receptor,CCK-AR,Cholecystokinin-1 receptor,CCK1-R |
5 | A | Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,with certain residues mutated to match Guanine nucleotide-binding protein G(q) subunit | polymer | 253 | 29145.0 | 1 | UniProt (P63096) UniProt (P63092) Pfam (PF00503) In PDB | Homo sapiens (Human) | Adenylate cyclase-inhibiting G alpha protein,Adenylate cyclase-stimulating G alpha protein,Adenylate cyclase-stimulating G alpha protein |
6 | R | CHOLESTEROL HEMISUCCINATE | non-polymer | 486.7 | 1 | Chemie (Y01) |
Sequence modifications
P: 1 - 8 (UniProt: P06307)
A: 9 - 37 (UniProt: P63096)
A: 38 - 195 (UniProt: P63092)
A: 204 - 394 (UniProt: P63092)
PDB | External Database | Details |
---|---|---|
Nh2 9 | - | amidation |
PDB | External Database | Details |
---|---|---|
His 1 | - | expression tag |
His 2 | - | expression tag |
His 3 | - | expression tag |
His 4 | - | expression tag |
His 5 | - | expression tag |
His 6 | - | expression tag |
His 7 | - | expression tag |
His 8 | - | expression tag |
PDB | External Database | Details |
---|---|---|
Arg 39 | Ala 39 | engineered mutation |
Leu 41 | His 41 | engineered mutation |
Asp 49 | Gly 49 | conflict |
Asn 50 | Glu 50 | conflict |
PDB | External Database | Details |
---|---|---|
Gly 196 | - | linker |
Gly 197 | - | linker |
Ser 198 | - | linker |
Gly 199 | - | linker |
Gly 200 | - | linker |
Ser 201 | - | linker |
Gly 202 | - | linker |
Gly 203 | - | linker |
Asp 249 | Ala 249 | conflict |
Asp 252 | Ser 252 | conflict |
- | Asn 254 | deletion |
- | Met 255 | deletion |
- | Val 256 | deletion |
- | Ile 257 | deletion |
- | Arg 258 | deletion |
- | Glu 259 | deletion |
- | Asp 260 | deletion |
- | Asn 261 | deletion |
- | Gln 262 | deletion |
- | Thr 263 | deletion |
Asp 272 | Leu 272 | conflict |
Lys 343 | Asp 343 | engineered mutation |
Val 346 | Leu 346 | engineered mutation |
Asp 347 | Arg 347 | engineered mutation |
Ile 358 | Tyr 358 | engineered mutation |
Ala 372 | Ile 372 | conflict |
Ile 375 | Val 375 | conflict |
Lys 380 | Arg 380 | engineered mutation |
Leu 384 | Gln 384 | engineered mutation |
Gln 385 | Arg 385 | engineered mutation |
Asn 387 | His 387 | engineered mutation |
Glu 390 | Gln 390 | engineered mutation |
Asn 392 | Glu 392 | engineered mutation |
Val 394 | Leu 394 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 5 |
Total formula weight | 123320.2 | |
Non-Polymers* | Number of molecules | 1 |
Total formula weight | 486.7 | |
All* | Total formula weight | 123806.9 |