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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OE6

Crystal structure of the CXCR4 chemokine receptor in complex with a small molecule antagonist IT1t in I222 spacegroup

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0019955	molecular_function	cytokine binding
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ITD A 1500

Chain	Residue
A	TRP94
A	ASP97
A	TYR116
A	ARG183
A	CYS186
A	ASP187
A	GLU288

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLC A 1600

Chain	Residue
A	VAL62
A	ILE269
A	ILE270
A	PRO299
A	TYR302
A	LEU305
A	LEU58
A	VAL59

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 1601

Chain	Residue
A	VAL99
A	ALA100
A	TYR103
A	ILE223

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 1602

Chain	Residue
A	LYS38
A	ILE39
A	PRO42
A	THR43
A	SER46

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1603

Chain	Residue
A	LEU120
A	SER123
A	VAL124
A	HIS203
A	GLY207
A	PHE248
A	TRP252
A	TYR256

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER122-ILE138

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	ILE39-MET63

site_id	SWS_FT_FI2
Number of Residues	36
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	GLY64-ARG77
A	SER131-LYS154

site_id	SWS_FT_FI3
Number of Residues	21
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	LEU78-VAL99

site_id	SWS_FT_FI4
Number of Residues	50
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	ALA100-LYS110
A	ALA175-TRP195
A	ASP262-LYS282

site_id	SWS_FT_FI5
Number of Residues	19
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	ALA111-ILE130

site_id	SWS_FT_FI6
Number of Residues	19
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	VAL155-PHE174

site_id	SWS_FT_FI7
Number of Residues	20
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	VAL196-LEU216

site_id	SWS_FT_FI8
Number of Residues	19
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	VAL242-ILE261

site_id	SWS_FT_FI9
Number of Residues	19
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:20929726

Chain	Residue	Details
A	TRP283-TYR302

site_id	SWS_FT_FI10
Number of Residues	1
Details	SITE: Chemokine binding

Chain	Residue	Details
A	ASP171

site_id	SWS_FT_FI11
Number of Residues	1
Details	SITE: Chemokine binding => ECO:0000269\|PubMed:20929726, ECO:0000305\|PubMed:10825158

Chain	Residue	Details
A	GLU288

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Sulfotyrosine; partial => ECO:0000269\|PubMed:18834145

Chain	Residue	Details
A	TYR7
A	TYR12

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Sulfotyrosine => ECO:0000269\|PubMed:12034737, ECO:0000269\|PubMed:16725153, ECO:0000269\|PubMed:18834145

Chain	Residue	Details
A	TYR21

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER319

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:20048153, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER321

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKC and GRK6 => ECO:0000269\|PubMed:19116316, ECO:0000269\|PubMed:20048153, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER324
A	SER325

site_id	SWS_FT_FI17
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10756055

Chain	Residue	Details
A	ASN11

site_id	SWS_FT_FI18
Number of Residues	1
Details	CARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine => ECO:0000269\|PubMed:12034737

Chain	Residue	Details
A	SER18

site_id	SWS_FT_FI19
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN176

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

237735

PDB entries from 2025-06-18

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