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3HVH

Rat catechol O-methyltransferase in complex with a catechol-type, N6-methyladenine-containing bisubstrate inhibitor

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 Residues32
DetailsBINDING SITE FOR RESIDUE 542 A 1
ChainResidue
ACXS3
AALA140
AGLN143
AGLN144
AGLY160
AALA161
ASER162
AGLN163
AASP184
AHIS185
ATRP186
AHOH43
ALYS187
AARG189
AASP212
AASN213
AVAL216
APRO217
ALEU241
AGLU242
AMG265
AHOH332
AMET83
AHOH337
AHOH369
AHOH379
AGLY109
ATYR111
AGLU133
AMET134
AASN135
ATYR138

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CXS A 3
ChainResidue
A5421
AHOH29
ALYS48
ATRP81
AALA139
AALA140
AGLN143
AILE157
AMET244
ASO4270
AHOH398
AHOH401
AHOH471

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CXS A 2
ChainResidue
ALEU195
AGLU198
ATYR225
ASER231
APHE232
ATYR240
ALYS245
APRO258
AHOH417
AHOH429
AHOH512

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 265
ChainResidue
A5421
AASP184
AASP212
AASN213
AHOH369

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 266
ChainResidue
ASER101
ASER103
AHOH294
AHOH344
AHOH371
AHOH454

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 267
ChainResidue
AVAL226
AARG227
ASER229
APHE232
AHOH291
AHOH509

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 268
ChainResidue
AASP87
AALA88
ATYR243
AHOH361

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 269
ChainResidue
APRO125
AGLY126
AARG128
ALYS154

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 270
ChainResidue
ACXS3
ATRP81
ALEU158
AASN159
AMET244
AHOH313
AHOH384
AHOH511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326
ChainResidueDetails
AASP184
AVAL85
ASER115
AGLU133

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
AMET134
ASER162
AGLU107

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS187
AASP212
AASN213
AGLU242
AGLY160

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER259
ASER260
ASER264

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 915
ChainResidueDetails
AASP184metal ligand
ALYS187proton shuttle (general acid/base)
AASP212metal ligand
AASN213metal ligand
AGLU242electrostatic stabiliser

221051

PDB entries from 2024-06-12

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