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6RZ8

Crystal structure of the human cysteinyl leukotriene receptor 2 in complex with ONO-2080365

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004974molecular_functionleukotriene receptor activity
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue KNZ A 2001
ChainResidue
ALYS37
ALEU198
AMET201
AGLY209
AARG267
ALEU271
AHIS284
AHOH2108
AHOH2111
AHOH2112
AHOH2113
ATYR119
ATYR127
AILE166
ASER169
ASER170
ALEU188
ALEU190
ALYS194

site_idAC2
Number of Residues7
Detailsbinding site for residue OLC A 2002
ChainResidue
ASER83
ASER89
APHE93
APHE106
AGLU1081
AOLC2006
AOLA2013

site_idAC3
Number of Residues10
Detailsbinding site for residue OLC A 2003
ChainResidue
AARG38
AGLU39
APRO42
AILE43
AILE47
AARG282
AALA286
AILE289
ALEU293
AOLC2011

site_idAC4
Number of Residues13
Detailsbinding site for residue OLC A 2004
ChainResidue
ALEU46
APHE49
APRO92
AASP96
ALEU99
AARG100
ATHR265
AVAL269
ACYS279
ALEU283
AOLC2010
AOLA2012
AHOH2101

site_idAC5
Number of Residues2
Detailsbinding site for residue OLC A 2005
ChainResidue
APHE36
AOLA2014

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 2006
ChainResidue
ALEU86
AOLC2002

site_idAC7
Number of Residues1
Detailsbinding site for residue OLC A 2007
ChainResidue
ATHR272

site_idAC8
Number of Residues4
Detailsbinding site for residue OLC A 2009
ChainResidue
ACYS299
APHE300
ALEU303
AOLC2011

site_idAC9
Number of Residues2
Detailsbinding site for residue OLC A 2010
ChainResidue
AVAL53
AOLC2004

site_idAD1
Number of Residues8
Detailsbinding site for residue OLC A 2011
ChainResidue
ALEU58
ASER59
AVAL62
APHE63
APRO302
ATYR305
AOLC2003
AOLC2009

site_idAD2
Number of Residues2
Detailsbinding site for residue OLA A 2012
ChainResidue
AASP96
AOLC2004

site_idAD3
Number of Residues3
Detailsbinding site for residue OLA A 2013
ChainResidue
AILE105
AGLU1081
AOLC2002

site_idAD4
Number of Residues2
Detailsbinding site for residue OLA A 2014
ChainResidue
ALYS285
AOLC2005

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AILE43-PHE63

site_idSWS_FT_FI2
Number of Residues16
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALEU64-SER72
AARG145-ARG153

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AVAL73-PHE93

site_idSWS_FT_FI4
Number of Residues77
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AARG94-TYR123
AASP175-ILE204
AARG267-ALA286

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ASER124-PHE144

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ASER154-LEU174

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AALA205-ILE225

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
ALEU246-LEU266

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
ALEU287-PHE307

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN20
AASN26
AASN30
AASN181

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

221716

PDB entries from 2024-06-26

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