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3HVJ

Rat catechol O-methyltransferase in complex with a catechol-type, N6-propyladenine-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
B0000287molecular_functionmagnesium ion binding
B0006584biological_processcatecholamine metabolic process
B0008171molecular_functionO-methyltransferase activity
B0016206molecular_functioncatechol O-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE 705 A 1
ChainResidue
AHOH40
ASER162
AGLN163
AASP184
AHIS185
ATRP186
ALYS187
AARG189
AASP212
AASN213
AGLU242
AMET83
AMG265
AHOH317
AHOH324
AHOH401
B7052
BTRP81
BLEU241
BMET244
AGLY109
ATYR111
AGLU133
AMET134
ATYR138
AGLY160
AALA161

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 265
ChainResidue
A7051
AASP184
AASP212
AASN213
AHOH401

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 266
ChainResidue
AASP87
AALA88
ATYR243

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BTB A 267
ChainResidue
ACYS76
ATHR77
ALYS79
ATRP81
AHOH433
B7052
BTRP186
BLYS187
BASP188
BPRO217
BHOH373

site_idAC5
Number of Residues30
DetailsBINDING SITE FOR RESIDUE 705 B 2
ChainResidue
A7051
ATRP81
ALEU241
AMET244
ABTB267
AHOH425
BTRP81
BMET83
BGLY109
BTYR111
BGLU133
BMET134
BASN135
BTYR138
BGLY160
BALA161
BSER162
BGLN163
BASP184
BHIS185
BTRP186
BLYS187
BARG189
BASP212
BASN213
BPRO217
BGLU242
BMG265
BHOH345
BHOH433

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 265
ChainResidue
B7052
BASP184
BASP212
BASN213
BHOH433

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326
ChainResidueDetails
AVAL85
ASER115
AGLU133
AASP184
BVAL85
BSER115
BGLU133
BASP184

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
AGLU107
AMET134
ASER162
BGLU107
BMET134
BSER162

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AGLY160
BGLU242
ALYS187
AASP212
AASN213
AGLU242
BGLY160
BLYS187
BASP212
BASN213

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER259
ASER260
ASER264
BSER259
BSER260
BSER264

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1vid
ChainResidueDetails
ALYS187
AGLU242

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1vid
ChainResidueDetails
BLYS187
BGLU242

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

site_idMCSA2
Number of Residues5
DetailsM-CSA 915
ChainResidueDetails
BASP184metal ligand
BLYS187proton shuttle (general acid/base)
BASP212metal ligand
BASN213metal ligand
BGLU242electrostatic stabiliser

219140

PDB entries from 2024-05-01

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