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6GPX

CRYSTAL STRUCTURE OF CCR2A IN COMPLEX WITH MK-0812

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004950molecular_functionchemokine receptor activity
A0005506molecular_functioniron ion binding
A0006935biological_processchemotaxis
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0043448biological_processalkane catabolic process
A0046872molecular_functionmetal ion binding
B0004930molecular_functionG protein-coupled receptor activity
B0004950molecular_functionchemokine receptor activity
B0005506molecular_functioniron ion binding
B0006935biological_processchemotaxis
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0043448biological_processalkane catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE264-GLY274

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 Residues54
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AGLN43-TYR70
BGLN43-TYR70

site_idSWS_FT_FI2
Number of Residues50
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS71-TYR80
AASP137-THR153
BLYS71-TYR80
BASP137-THR153

site_idSWS_FT_FI3
Number of Residues38
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
ALEU81-HIS100
BLEU81-HIS100

site_idSWS_FT_FI4
Number of Residues112
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ASER101-LYS114
ATHR179-ARG206
AGLN320-GLN336
BSER101-LYS114
BTHR179-ARG206
BGLN269-GLN285

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU115-ILE136
BLEU115-ILE136

site_idSWS_FT_FI6
Number of Residues48
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AVAL154-PHE178
BVAL154-PHE178

site_idSWS_FT_FI7
Number of Residues38
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AASN207-LEU226
BASN207-LEU226

site_idSWS_FT_FI8
Number of Residues48
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AVAL295-PHE319
BVAL244-PHE268

site_idSWS_FT_FI9
Number of Residues46
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AALA337-GLY360
BALA286-GLY309

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:9670957
ChainResidueDetails
ATYR139
BTYR139

site_idSWS_FT_FI11
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292
ChainResidueDetails
ACYS237
ACYS240
ACYS270
ACYS273
BCYS229
BCYS229
BCYS230
BCYS230

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309
ChainResidueDetails
AMET232
BMET229

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PDB entries from 2024-07-24

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