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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EML

The 2.6 A Crystal Structure of a Human A2A Adenosine Receptor bound to ZM241385.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme 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	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
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	11
Details	BINDING SITE FOR RESIDUE ZMA A 401

Chain	Residue
A	PHE168
A	HOH519
A	HOH559
A	GLU169
A	MET177
A	TRP246
A	LEU249
A	HIS250
A	ASN253
A	HIS264
A	MET270

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE STE A 402

Chain	Residue
A	VAL57
A	LEU58
A	STE405
A	HOH570

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE STE A 403

Chain	Residue
A	VAL46

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE STE A 404

Chain	Residue
A	VAL57
A	PHE62
A	STE405

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE STE A 405

Chain	Residue
A	GLY76
A	ILE80
A	STE402
A	STE404

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE STE A 406

Chain	Residue
A	GLY23
A	PHE299
A	HOH562

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 407

Chain	Residue
A	ARG222
A	HOH506
A	ASN1040
A	THR1157
A	TRP1158

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 408

Chain	Residue
A	ARG296
A	GLN297
A	ARG300

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	ARG107
A	ALA203
A	ARG206
A	HOH530
A	ARG1008

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 410

Chain	Residue
A	ALA73
A	CYS74
A	HIS75

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 411

Chain	Residue
A	THR1142
A	PRO1143
A	ASN1144
A	ARG1145

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 412

Chain	Residue
A	PHE1114
A	THR1115
A	ASN1116
A	SER1117
A	ASN1132

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 413

Chain	Residue
A	HOH547
A	ARG1076
A	ARG1080

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. SSIfSLLAIAIDRYIaI

Chain	Residue	Details
A	SER90-ILE106

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	TRANSMEM: Helical; Name=1

Chain	Residue	Details
A	VAL8-TRP32

site_id	SWS_FT_FI2
Number of Residues	28
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:18832607

Chain	Residue	Details
A	LEU33-ASN42
A	ASP101-ARG120

site_id	SWS_FT_FI3
Number of Residues	23
Details	TRANSMEM: Helical; Name=2

Chain	Residue	Details
A	TYR43-ILE66

site_id	SWS_FT_FI4
Number of Residues	46
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:18832607

Chain	Residue	Details
A	SER67-CYS77
A	ASN144-PRO173
A	CYS259-PRO266

site_id	SWS_FT_FI5
Number of Residues	22
Details	TRANSMEM: Helical; Name=3

Chain	Residue	Details
A	LEU78-ILE100

site_id	SWS_FT_FI6
Number of Residues	22
Details	TRANSMEM: Helical; Name=4

Chain	Residue	Details
A	ALA121-TRP143

site_id	SWS_FT_FI7
Number of Residues	24
Details	TRANSMEM: Helical; Name=5

Chain	Residue	Details
A	MET174-LEU198

site_id	SWS_FT_FI8
Number of Residues	23
Details	TRANSMEM: Helical; Name=6

Chain	Residue	Details
A	LEU235-PHE258

site_id	SWS_FT_FI9
Number of Residues	23
Details	TRANSMEM: Helical; Name=7

Chain	Residue	Details
A	LEU267-TYR290

site_id	SWS_FT_FI10
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:21593763, ECO:0007744\|PDB:2YDO

Chain	Residue	Details
A	GLU169
A	ASN253
A	SER277
A	HIS278

site_id	SWS_FT_FI11
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN154

site_id	SWS_FT_FI12
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	GLU1011

site_id	SWS_FT_FI13
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASP1020

site_id	SWS_FT_FI14
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU1032
A	PHE1104

site_id	SWS_FT_FI15
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER1117
A	ASN1132

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 206l

Chain	Residue	Details
A	ASP1020
A	GLU1011

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

222415

PDB entries from 2024-07-10

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