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6I3D

Crystal structure of Human soluble catechol O-methyltransferase in complex with 3,5-dinitrocatechol and Sinefungin

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 Residues13
Detailsbinding site for residue DNC A 301
ChainResidue
ATRP38
AGLU199
AMG302
ASFG303
AHOH427
AMET40
AASP141
AHIS142
ATRP143
ALYS144
AASP169
AASN170
APRO174

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AASP141
AASP169
AASN170
ADNC301
AHOH427

site_idAC3
Number of Residues20
Detailsbinding site for residue SFG A 303
ChainResidue
AMET40
AASN41
AVAL42
AGLY66
AALA67
ATYR68
ATYR71
ASER72
AILE89
AGLU90
AILE91
ASER119
AGLN120
AASP141
AHIS142
ATRP143
ADNC301
AHOH434
AHOH458
AHOH532

site_idAC4
Number of Residues14
Detailsbinding site for residue DNC B 301
ChainResidue
BTRP38
BMET40
BASP141
BHIS142
BTRP143
BLYS144
BASP169
BASN170
BPRO174
BLEU198
BGLU199
BMG302
BSFG303
BHOH419

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 302
ChainResidue
BASP141
BASP169
BASN170
BDNC301
BHOH419

site_idAC6
Number of Residues23
Detailsbinding site for residue SFG B 303
ChainResidue
BMET40
BASN41
BVAL42
BGLY66
BALA67
BTYR68
BTYR71
BSER72
BILE89
BGLU90
BILE91
BGLY117
BALA118
BSER119
BGLN120
BASP141
BHIS142
BTRP143
BARG146
BDNC301
BHOH425
BHOH477
BHOH525

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:18486144
ChainResidueDetails
BGLU90
BASP141
AVAL42
ASER72
AGLU90
AASP141
BVAL42
BSER72

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
ASER119
BGLU64
BILE91
BSER119
AGLU64
AILE91

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASN170
AGLU199
BGLY117
BLYS144
BASN170
BGLU199
ALYS144
AGLY117

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18486144
ChainResidueDetails
AASP169
BASP169

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P22734
ChainResidueDetails
ASER217
BSER217

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PDB entries from 2024-05-15

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