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5PA0

humanized rat COMT in complex with 3-hydroxy-1-methyl-5-phenylpyridin-2-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006584biological_processcatecholamine metabolic process
A0008171molecular_functionO-methyltransferase activity
A0016206molecular_functioncatechol O-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue SAH A 301
ChainResidue
ASME40
AGLU90
AILE91
AGLY117
AALA118
ASER119
AGLN120
AASP141
AHIS142
ATRP143
AARG146
AASN41
AHOH445
AHOH484
AHOH555
AVAL42
AGLY66
AALA67
ATYR68
ATYR71
ASER72
AMET89

site_idAC2
Number of Residues11
Detailsbinding site for residue 7JR A 302
ChainResidue
ASME40
AALA97
AGLN101
AASP141
ALYS144
AASP169
AASN170
AGLU199
ASO4309
AMG310
AHOH442

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
AASP44
AALA45
ATYR200
AHOH578

site_idAC4
Number of Residues9
Detailsbinding site for residue CXS A 304
ChainResidue
ALYS5
ATRP38
AGLN100
AILE114
AMET201
ASO4308
AHOH458
AHOH459
AHOH543

site_idAC5
Number of Residues9
Detailsbinding site for residue CXS A 305
ChainResidue
AGLU155
ATYR182
ASER188
ALYS202
APRO215
AHOH408
AHOH437
AHOH471
AHOH478

site_idAC6
Number of Residues6
Detailsbinding site for residue CXS A 306
ChainResidue
AARG8
ALYS36
AGLU37
AHOH451
AHOH566
AHOH601

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 A 307
ChainResidue
AGLY83
AARG85
ALYS111
ALYS128
AHOH413
AHOH425
AHOH564

site_idAC8
Number of Residues8
Detailsbinding site for residue SO4 A 308
ChainResidue
AGLU37
ATRP38
ALEU115
AASN116
ACXS304
AHOH414
AHOH435
AHOH467

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 A 309
ChainResidue
ATRP143
ALYS144
A7JR302
AHOH401
AHOH402
AHOH585

site_idAD1
Number of Residues5
Detailsbinding site for residue MG A 310
ChainResidue
AASP141
AASP169
AASN170
A7JR302
AHOH442

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326
ChainResidueDetails
AVAL42
ASER72
AGLU90
AASP141

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
AGLU64
AILE91
ASER119

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLY117
ALYS144
AASP169
AASN170
AGLU199

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER216
ASER217
ASER221

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 915
ChainResidueDetails
AASP141metal ligand
ALYS144proton shuttle (general acid/base)
AASP169metal ligand
AASN170metal ligand
AGLU199electrostatic stabiliser

223790

PDB entries from 2024-08-14

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