Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MBS

Crystal Structure of the CCR5 Chemokine Receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004950	molecular_function	chemokine receptor activity
A	0005506	molecular_function	iron ion binding
A	0006935	biological_process	chemotaxis
A	0006954	biological_process	inflammatory response
A	0006955	biological_process	immune response
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0016493	molecular_function	C-C chemokine receptor activity
A	0043448	biological_process	alkane catabolic process
A	0046872	molecular_function	metal ion binding
B	0004930	molecular_function	G protein-coupled receptor activity
B	0004950	molecular_function	chemokine receptor activity
B	0005506	molecular_function	iron ion binding
B	0006935	biological_process	chemotaxis
B	0006954	biological_process	inflammatory response
B	0006955	biological_process	immune response
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0009055	molecular_function	electron transfer activity
B	0016020	cellular_component	membrane
B	0016493	molecular_function	C-C chemokine receptor activity
B	0043448	biological_process	alkane catabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MRV A 1101

Chain	Residue
A	TYR37
A	THR259
A	GLU283
A	TRP86
A	TYR89
A	TYR108
A	PHE109
A	PHE182
A	THR195
A	TRP248
A	TYR251

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1102

Chain	Residue
A	CYS1006
A	CYS1009
A	CYS1039
A	CYS1042

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC A 1103

Chain	Residue
A	PHE158
B	PRO35

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 1104

Chain	Residue
A	PRO84
A	PHE85
A	HIS88
A	OLC1105
A	HOH1219

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 1105

Chain	Residue
A	SER38
A	PRO84
A	HIS88
A	OLC1104

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 1106

Chain	Residue
A	PHE78
A	THR99
A	GLN102
A	TRP153
A	HOH1212

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 1107

Chain	Residue
A	LEU33
A	VAL281
A	THR284
A	LEU285
A	THR288

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC A 1108

Chain	Residue
A	TYR214
A	ARG235
A	PHE238

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MRV B 1101

Chain	Residue
B	TYR37
B	TRP86
B	TYR89
B	TYR108
B	PHE109
B	PHE182
B	LYS191
B	THR195
B	TRP248
B	TYR251
B	THR259
B	GLU283

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1102

Chain	Residue
B	CYS1006
B	CYS1009
B	CYS1039
B	CYS1042

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE OLC B 1103

Chain	Residue
B	OLC1105

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC B 1104

Chain	Residue
B	ALA30
B	PRO34
B	SER38
B	HOH1210

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC B 1105

Chain	Residue
B	ALA278
B	OLC1103

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC B 1106

Chain	Residue
B	VAL234
B	ARG235
B	PHE238
B	HOH1226

Functional Information from PROSITE/UniProt

site_id	PS00202
Number of Residues	11
Details	RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG

Chain	Residue	Details
A	ILE1033-GLY1043

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SGIfFIILLTIDRYLaV

Chain	Residue	Details
A	SER114-VAL130

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	106
Details	Domain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	54
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	50
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	118
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	42
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	38
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	46
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)