Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8K3Z

Cryo-EM structure of CXCR4 in complex with CXCL12

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0001750	cellular_component	photoreceptor outer segment
B	0003924	molecular_function	GTPase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005765	cellular_component	lysosomal membrane
B	0005829	cellular_component	cytosol
B	0005834	cellular_component	heterotrimeric G-protein complex
B	0005886	cellular_component	plasma membrane
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
B	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
B	0007213	biological_process	G protein-coupled acetylcholine receptor signaling pathway
B	0007265	biological_process	Ras protein signal transduction
B	0008283	biological_process	cell population proliferation
B	0016020	cellular_component	membrane
B	0030159	molecular_function	signaling receptor complex adaptor activity
B	0044877	molecular_function	protein-containing complex binding
B	0045202	cellular_component	synapse
B	0050909	biological_process	sensory perception of taste
B	0051020	molecular_function	GTPase binding
B	0060041	biological_process	retina development in camera-type eye
B	0070062	cellular_component	extracellular exosome
B	0071380	biological_process	cellular response to prostaglandin E stimulus
B	0071870	biological_process	cellular response to catecholamine stimulus
B	0097381	cellular_component	photoreceptor disc membrane
B	1903561	cellular_component	extracellular vesicle
C	0000287	molecular_function	magnesium ion binding
C	0001664	molecular_function	G protein-coupled receptor binding
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005765	cellular_component	lysosomal membrane
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0005856	cellular_component	cytoskeleton
C	0005886	cellular_component	plasma membrane
C	0005938	cellular_component	cell cortex
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
C	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
C	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
C	0010854	molecular_function	adenylate cyclase regulator activity
C	0016787	molecular_function	hydrolase activity
C	0019003	molecular_function	GDP binding
C	0030496	cellular_component	midbody
C	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
C	0031749	molecular_function	D2 dopamine receptor binding
C	0031821	molecular_function	G protein-coupled serotonin receptor binding
C	0034695	biological_process	response to prostaglandin E
C	0043434	biological_process	response to peptide hormone
C	0043949	biological_process	regulation of cAMP-mediated signaling
C	0045542	biological_process	positive regulation of cholesterol biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0051301	biological_process	cell division
C	0060236	biological_process	regulation of mitotic spindle organization
C	0070062	cellular_component	extracellular exosome
C	0072678	biological_process	T cell migration
C	1904322	biological_process	cellular response to forskolin
C	1904778	biological_process	positive regulation of protein localization to cell cortex

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. SSVlILAFISLDRYLaI

Chain	Residue	Details
A	SER122-ILE138

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS

Chain	Residue	Details
B	LEU70-SER84
B	ILE157-ILE171
B	LEU285-ALA299

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
D	ARG20
D	ARG41
D	GLN48

site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Important for integrin interaction and activation => ECO:0000269\|PubMed:29301984

Chain	Residue	Details
D	LYS24
D	LYS27
D	LYS43

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Important for dimer formation

Chain	Residue	Details
D	HIS25

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
C	LEU175
A	ALA175-TRP195
A	ASP262-LYS282

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
C	ASP200

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
C	ALA326

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
C	ARG178

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
C	GLN204

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
C	CYS351

site_id	SWS_FT_FI10
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:20213681, ECO:0000269\|PubMed:25255805

Chain	Residue	Details
C	GLY2

site_id	SWS_FT_FI11
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000250\|UniProtKB:P10824

Chain	Residue	Details
C	CYS3

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER319

site_id	SWS_FT_FI13
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN176

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)