9ASB
Structure of human calcium-sensing receptor in complex with chimeric Gq (miniGisq) protein in nanodiscs
This is a non-PDB format compatible entry.
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | Q, R | Isoform 1 of Extracellular calcium-sensing receptor | polymer | 911 | 102864.6 | 2 | UniProt (P41180) Pfam (PF01094) Pfam (PF07562) Pfam (PF00003) In PDB | Homo sapiens (human) | CaR,CaSR,hCasR,Parathyroid cell calcium-sensing receptor 1,PCaR1 |
2 | A | Chimeric mini guanine nucleotide-binding protein G(i)(s)(q) subunit alpha | polymer | 246 | 28306.1 | 1 | UniProt (P63096) UniProt (A0A590UJY2) Pfam (PF00503) In PDB | Homo sapiens (human) | Adenylate cyclase-inhibiting G alpha protein |
3 | B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | polymer | 348 | 38413.9 | 1 | UniProt (P62873) Pfam (PF00400) In PDB | Homo sapiens (human) | Transducin beta chain 1 |
4 | G | Chimeric mini guanine nucleotide-binding protein G(i)(s)(q) subunit alpha | polymer | 71 | 7861.1 | 1 | UniProt (P59768) Pfam (PF00631) In PDB | Homo sapiens (human) | G gamma-I |
5 | C, D, E, F | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 424.4 | 4 | In PDB GlyTouCan (G42666HT) | |||
6 | Q, R | 2-acetamido-2-deoxy-beta-D-glucopyranose | non-polymer | 221.2 | 6 | Chemie (NAG) | |||
7 | Q, R | CYCLOMETHYLTRYPTOPHAN | non-polymer | 216.2 | 2 | Chemie (TCR) | |||
8 | Q, R | PHOSPHATE ION | non-polymer | 95.0 | 2 | Chemie (PO4) | |||
9 | R, Q | CALCIUM ION | non-polymer | 40.1 | 6 | Chemie (CA) | |||
10 | R, Q | 3-(2-chlorophenyl)-N-[(1R)-1-(3-methoxyphenyl)ethyl]propan-1-amine | non-polymer | 303.8 | 2 | Chemie (9IG) | |||
11 | Q | CHOLESTEROL HEMISUCCINATE | non-polymer | 486.7 | 1 | Chemie (Y01) | |||
12 | R | (19R,22S,25R)-22,25,26-trihydroxy-16,22-dioxo-17,21,23-trioxa-22lambda~5~-phosphahexacosan-19-yl (9Z)-octadec-9-enoate | non-polymer | 749.0 | 1 | Chemie (A1AF7) |
Sequence modifications
Q, R: -7 - 903 (UniProt: P41180)
A: 1 - 53 (UniProt: P63096)
A: 69 - 246 (UniProt: A0A590UJY2)
B: 2 - 340 (UniProt: P62873)
PDB | External Database | Details |
---|---|---|
Asp 12 | - | insertion |
Tyr 13 | - | insertion |
Lys 14 | - | insertion |
Asp 15 | - | insertion |
Asp 16 | - | insertion |
Asp 17 | - | insertion |
Asp 18 | - | insertion |
Lys 19 | - | insertion |
PDB | External Database | Details |
---|---|---|
Glu 20 | Asp 20 | engineered mutation |
Lys 21 | Arg 21 | engineered mutation |
Gln 22 | Asn 22 | engineered mutation |
Gln 24 | Arg 24 | engineered mutation |
Lys 25 | Glu 25 | engineered mutation |
Lys 27 | Gly 27 | engineered mutation |
Gln 28 | Glu 28 | engineered mutation |
Val 29 | Lys 29 | engineered mutation |
Tyr 30 | Ala 30 | engineered mutation |
Arg 31 | Ala 31 | engineered mutation |
Ala 32 | Arg 32 | engineered mutation |
Thr 33 | Glu 33 | engineered mutation |
His 34 | Val 34 | engineered mutation |
Arg 35 | Lys 35 | engineered mutation |
Asp 42 | Gly 42 | engineered mutation |
Asn 43 | Glu 43 | engineered mutation |
Arg 54 | - | linker |
Ile 55 | - | linker |
Leu 56 | - | linker |
His 57 | - | linker |
Gly 58 | - | linker |
Gly 59 | - | linker |
Ser 60 | - | linker |
Gly 61 | - | linker |
Gly 62 | - | linker |
Ser 63 | - | linker |
Gly 64 | - | linker |
Gly 65 | - | linker |
Thr 66 | - | linker |
Ser 67 | - | linker |
Gly 68 | - | linker |
PDB | External Database | Details |
---|---|---|
Asp 111 | Ala 92 | engineered mutation |
Asp 114 | Ser 95 | engineered mutation |
- | Asn 97 | deletion |
- | Met 98 | deletion |
- | Val 99 | deletion |
- | Ile 100 | deletion |
- | Arg 101 | deletion |
- | Glu 102 | deletion |
- | Asp 103 | deletion |
- | Asn 104 | deletion |
- | Gln 105 | deletion |
- | Thr 106 | deletion |
Asp 124 | Leu 115 | engineered mutation |
Ala 224 | Ile 215 | engineered mutation |
Ile 227 | Val 218 | engineered mutation |
Lys 232 | Arg 223 | engineered mutation |
Leu 236 | Gln 227 | engineered mutation |
Gln 237 | Arg 228 | engineered mutation |
Asn 239 | His 230 | engineered mutation |
Glu 242 | Gln 233 | engineered mutation |
Asn 244 | Glu 235 | engineered mutation |
Val 246 | Leu 237 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Met -7 | - | initiating methionine |
Asp -6 | - | expression tag |
Tyr -5 | - | expression tag |
Lys -4 | - | expression tag |
Asp -3 | - | expression tag |
Asp -2 | - | expression tag |
Asp -1 | - | expression tag |
Asp 0 | - | expression tag |
Lys 1 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 5 |
Total formula weight | 280310.4 | |
Branched | Number of molecules | 4 |
Total formula weight | 1697.6 | |
Non-Polymers* | Number of molecules | 20 |
Total formula weight | 4033.5 | |
All* | Total formula weight | 286041.5 |