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9C1P

Structure of Calcium-Sensing Receptor in complex with positive allosteric modulator '6218

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00979
Number of Residues19
DetailsG_PROTEIN_RECEP_F3_1 G-protein coupled receptors family 3 signature 1. VaNLLgLFyIPQVSyASSS
ChainResidueDetails
AVAL153-SER171
BVAL153-SER171

site_idPS00980
Number of Residues25
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCFeCveCpdgeYsdet.DasACnkC
ChainResidueDetails
ACYS561-CYS585
BCYS561-CYS585

site_idPS00981
Number of Residues11
DetailsG_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKfITFSM
ChainResidueDetails
APHE801-MET811
BPHE801-MET811

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues632
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BTYR20-PHE612
BGLU671-GLN681
BALA746-SER769
BTYR829-VAL836

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
BGLY613-ILE635

site_idSWS_FT_FI3
Number of Residues48
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BLYS636-GLU649
BARG701-GLN724
BLYS793-LYS805

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
BLEU650-GLY670

site_idSWS_FT_FI5
Number of Residues18
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
BPRO682-ASN700

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
BPHE725-THR745

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
BLEU770-PHE792

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
BPHE806-THR828

site_idSWS_FT_FI9
Number of Residues25
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
BGLU837-PHE862

site_idSWS_FT_FI10
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5K5S
ChainResidueDetails
BARG66
BTHR145
BGLU231
BASP234
BARG415
BGLY557

site_idSWS_FT_FI11
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
BILE81
BLEU87
BLEU88

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0000305|PubMed:27386547, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
BSER84

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5K5S, ECO:0007744|PDB:5K5T
ChainResidueDetails
BTHR100

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27386547, ECO:0000269|PubMed:27434672, ECO:0007744|PDB:5FBH, ECO:0007744|PDB:5FBK, ECO:0007744|PDB:5K5S
ChainResidueDetails
BSER147
BALA168
BSER170
BGLU297

site_idSWS_FT_FI15
Number of Residues1
DetailsSITE: Important for ability of agonist AMG 416 to activate G-protein-coupled receptor activity => ECO:0000269|PubMed:26290606
ChainResidueDetails
BCYS482

site_idSWS_FT_FI16
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN90
BASN130
BASN386
BASN400

site_idSWS_FT_FI17
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:27434672
ChainResidueDetails
BASN261
BASN287
BASN446
BASN468
BASN488
BASN541
BASN594

226707

PDB entries from 2024-10-30

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