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2ZTH

Crystal structure of holo form of rat catechol-o-methyltransferase

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 Residues3
DetailsBINDING SITE FOR RESIDUE MG A 300
ChainResidue
AASP141
AASP169
AASN170

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAM A 305
ChainResidue
AGLU90
AMET91
ATYR95
AGLY117
AALA118
ASER119
AGLN120
AASP141
AHIS142
ATRP143
AARG146
AHOH358
AVAL42
AGLY66
AALA67
ATYR68
ATYR71
ASER72

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
AMET91
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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1vid
ChainResidueDetails
AGLU199
ALYS144

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

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PDB entries from 2024-07-17

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