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

5VBL

Structure of apelin receptor in complex with agonist peptide

Functional Information from GO Data
ChainGOidnamespacecontents
B0004930molecular_functionG protein-coupled receptor activity
B0005506molecular_functioniron ion binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0043448biological_processalkane catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 1101
ChainResidue
BCYS1006
BCYS1009
BCYS1039
BCYS1042

site_idAC2
Number of Residues8
Detailsbinding site for residue OLC B 1102
ChainResidue
BLEU201
BGLY202
BLYS268
BPHE110
BTYR114
BLEU160
BPRO163
BVAL164

site_idAC3
Number of Residues8
Detailsbinding site for residues HRG A 8 and ALC A 9
ChainResidue
AARG6
APRO7
AGLU10
BGLU20
BTYR21
BTHR22
BASP23
BASN175

site_idAC4
Number of Residues7
Detailsbinding site for residues OIC A 14 and NLE A 15
ChainResidue
ALYS13
APRO16
A20017
BMET183
BGLU198
BTYR271
BPHE291

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues33
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGLGVSSTTVgFvvpftimltcyffiaqt.IAMK
ChainResidueDetails
BVAL199-LYS1002

site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
BILE1033-GLY1043

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASAfCLTGLSFDRYLaI
ChainResidueDetails
BALA115-ILE131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
BSER27-TRP51

site_idSWS_FT_FI2
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BTHR52-ILE66
BASP126-VAL144

site_idSWS_FT_FI3
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
BPHE67-ARG91

site_idSWS_FT_FI4
Number of Residues53
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BASP92-PHE100
BLEU167-GLY200
BMET272-ASP284

site_idSWS_FT_FI5
Number of Residues24
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
BPHE101-PHE125

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
BSER145-VAL166

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
BLEU201-TYR221

site_idSWS_FT_FI8
Number of Residues26
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
BARG245-TYR271

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
BLEU285-LEU308

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN15
BASN175

site_idSWS_FT_FI11
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292
ChainResidueDetails
BCYS1006
BCYS1009
BCYS1039
BCYS1042

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309
ChainResidueDetails
BMET1001

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon