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5T1A

Structure of CC Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 73R A 1201
ChainResidue
AVAL37
AGLN288
AVAL289
AGLU291
ATHR292
AMET295
AGLY41
ALEU44
ALEU45
ATYR49
ATRP98
ATHR117
ATYR120
ACYS190

site_idAC2
Number of Residues10
Detailsbinding site for residue VT5 A 1202
ChainResidue
AVAL63
ATHR77
AARG237
AALA241
AVAL244
ATYR305
AGLY309
AGLU310
ALYS311
APHE312

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 1203
ChainResidue
ALYS71
ALYS311
AARG314
ATYR315
ALYS1135

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 1204
ChainResidue
ASER236
AARG237
AARG1008
AARG1119
AARG1125

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 1205
ChainResidue
APHE1114
ATHR1115
AASN1116
ASER1117
AASN1132

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 A 1206
ChainResidue
ATHR1142
APRO1143
AASN1144
AARG1145

site_idAC7
Number of Residues10
Detailsbinding site for residue OLC A 1207
ChainResidue
APHE170
ALYS180
ATRP198
AMET205
ATYR222
AARG232
ALYS239
AARG243
APHE246
ATHR247

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 1208
ChainResidue
AHIS144
AGLU238
AGLU1005
AHOH1307

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GGIfFIILLTIDRYLaI
ChainResidueDetails
AGLY126-ILE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues27
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AGLN43-CYS70

site_idSWS_FT_FI2
Number of Residues25
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS71-TYR80
AASP137-THR153

site_idSWS_FT_FI3
Number of Residues19
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
ALEU81-HIS100

site_idSWS_FT_FI4
Number of Residues56
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ASER101-LYS114
ATHR179-ARG206
AGLN269-GLN285

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU115-ILE136

site_idSWS_FT_FI6
Number of Residues24
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AVAL154-PHE178

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AASN207-SER226

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AVAL244-PHE268

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AALA286-GLY309

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:11046064
ChainResidueDetails
ATYR26

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:9670957
ChainResidueDetails
ATYR139

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN14

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI14
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI16
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

219140

PDB entries from 2024-05-01

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