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6GPS

CRYSTAL STRUCTURE OF CCR2A IN COMPLEX WITH MK-0812

Functional Information from GO Data
ChainGOidnamespacecontents
A0001974biological_processblood vessel remodeling
A0004930molecular_functionG protein-coupled receptor activity
A0004950molecular_functionchemokine receptor activity
A0005506molecular_functioniron ion binding
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0006955biological_processimmune response
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016493molecular_functionC-C chemokine receptor activity
A0043448biological_processalkane catabolic process
A0046872molecular_functionmetal ion binding
A0090026biological_processpositive regulation of monocyte chemotaxis
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 1101
ChainResidue
ACYS1006
ACYS1009
ACYS1039
ACYS1042
AVAL1044

site_idAC2
Number of Residues15
Detailsbinding site for residue F7N A 1102
ChainResidue
ALEU45
ATYR49
ATRP98
ATHR117
AHIS121
ACYS190
AGLN288
AVAL289
AGLU291
ATHR292
AMET295
AVAL37
AILE40
AGLY41
ALEU44

Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE1033-GLY1043

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 Residues53
DetailsDomain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues25
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by JAK2","evidences":[{"source":"PubMed","id":"9670957","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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