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4PYM

humanized rat apo-COMT bound to sulphate

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 Residues6
DetailsBINDING SITE FOR RESIDUE K A 301
ChainResidue
AVAL226
AARG227
ASER229
APHE232
AHOH423
AHOH591

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLY113
ATYR114
ASER115
AHOH407
AHOH550
AHOH551
AHOH589
AALA110
ATYR111
ACYS112

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

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
AGLU107
AILE134
ASER162

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

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

227344

PDB entries from 2024-11-13

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