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

6J21

Crystal structure of the human NK1 substance P receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0004995molecular_functiontachykinin receptor activity
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue GBQ A 1201
ChainResidue
AASN109
ATHR201
ATRP261
APHE264
APHE268
APRO112
AILE113
AVAL116
AILE182
ATRP184
AGLU193
AHIS197
AVAL200

site_idAC2
Number of Residues2
Detailsbinding site for residue OLC A 1202
ChainResidue
AGLY213
AGLY220

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwSMTAVAFDRYMaI
ChainResidueDetails
AALA118-ILE134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AILE32-MET54

site_idSWS_FT_FI2
Number of Residues28
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATRP55-ARG64
AASP129-LYS148

site_idSWS_FT_FI3
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
ATHR65-THR86

site_idSWS_FT_FI4
Number of Residues55
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AVAL87-LYS106
ATHR170-LYS194
APRO271-ILE283

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
APHE107-PHE128

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AVAL149-SER169

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AVAL195-VAL219

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AMET249-LEU270

site_idSWS_FT_FI9
Number of Residues24
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AGLN284-LEU308

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8384323
ChainResidueDetails
AHIS197

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ACYS322

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN14
AASN18

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
APHE1060

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1073
AASN1088

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 921
ChainResidueDetails

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon