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4DKL

Crystal structure of the mu-opioid receptor bound to a morphinan antagonist

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0008152biological_processmetabolic process
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BF0 A 601
ChainResidue
AASP147
ATRP318
AILE322
ATYR326
AHOH718
ATYR148
AMET151
AGLU229
ALYS233
AVAL236
ATRP293
AILE296
AVAL300

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
ATHR101
AALA102
ATHR103
AARG179
AILE278
AHOH701
AHOH712

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AASN137
ALYS141
ATHR207
AARG1119

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
AHIS171
APRO172
AVAL173
ALYS174
AGLY1012
ALEU1013

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
AARG1014
ALEU1015
ALYS1016

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 606
ChainResidue
AHIS223
APRO224
ATHR225
ATRP226

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 607
ChainResidue
AHIS223
AHOH714
AHOH722
AGLY1113
APHE1114
ATHR1115
AASN1116
ASER1117
AASN1132

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 608
ChainResidue
AHOH714
AARG1137

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 609
ChainResidue
APHE204
AARG1119
AGLN1123

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 610
ChainResidue
AARG277
AARG280

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 611
ChainResidue
AHIS171
AARG258
AARG1008
ALEU1013
ALYS1060

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 612
ChainResidue
ATHR1142
AASN1144
AARG1145

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 613
ChainResidue
AARG95
ATYR96
ATHR97

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CLR A 614
ChainResidue
ATYR299
AILE302
AILE308
ASER317
AHOH731

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPG A 615
ChainResidue
APHE108
AASN109
ALYS185
AASN188
ATRP192

site_idBC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MPG A 616
ChainResidue
AMET72
AMET72
AALA73
ATYR75
ASER76
ASER76
ACYS79
ALEU83
APRO122
ASER125

site_idBC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1PE A 617
ChainResidue
ATRP226
ATRP226
ALYS303
ALYS303
ALEU305
ALEU305
AILE306
AILE306
ATHR307
ATHR307

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 618
ChainResidue
ASER261
AGLU270

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLCTMSVDRYIaV
ChainResidueDetails
ATHR153-VAL169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
ATHR67-TYR91

site_idSWS_FT_FI2
Number of Residues31
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AVAL92-ASN104
AASP164-ASN183

site_idSWS_FT_FI3
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AILE105-LEU129

site_idSWS_FT_FI4
Number of Residues39
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AMET130-CYS140
AALA206-TRP228
ALEU305-THR312

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
ALYS141-VAL163

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AALA184-MET205

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AGLU229-GLY253

site_idSWS_FT_FI8
Number of Residues26
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
AILE278-ALA304

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
ChainResidueDetails
APHE313-TYR336

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P33535
ChainResidueDetails
ATYR166

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ACYS351

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_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
ChainResidueDetails
AASN1020

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASN1020covalent catalysis

218853

PDB entries from 2024-04-24

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