Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7XN9

Crystal structure of SSTR2 and L-054,522 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004930molecular_functionG protein-coupled receptor activity
A0004994molecular_functionsomatostatin receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfCLTVMSIDRYLaV
ChainResidueDetails
ATHR128-VAL144

site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
APRO1074-TRP1084

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
AMET1168-SER1179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AALA44-VAL67

site_idSWS_FT_FI2
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AILE68-THR78
AASP139-MET161

site_idSWS_FT_FI3
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AASN79-VAL103

site_idSWS_FT_FI4
Number of Residues48
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA104-VAL118
AGLY182-GLY207
ASER279-PRO288

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AMET119-ILE138

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AILE162-ALA181

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
APHE208-LEU229

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AVAL254-SER278

site_idSWS_FT_FI9
Number of Residues14
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AALA289-ALA303

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Important for ligand binding
ChainResidueDetails
AASP89

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P30680
ChainResidueDetails
ASER341
ASER343
ASER348

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P30680
ChainResidueDetails
ATHR353
ATHR354

site_idSWS_FT_FI13
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ACYS328

site_idSWS_FT_FI14
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN9
AASN22
AASN29
AASN32

site_idSWS_FT_FI15
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU1077

site_idSWS_FT_FI16
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU1171

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
AASN1034modifies pKa
ATYR1068electrostatic destabiliser
AGLU1077covalent catalysis, proton shuttle (general acid/base)
ATYR1079modifies pKa
AGLU1171proton shuttle (general acid/base)

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon