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5FHR

Crystal structure of Y200L mutant of Rat Catechol-O-Methyltransferase in complex with AdoMet and 3,5-dinitrocatechol

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 Residues11
Detailsbinding site for residue DNC A 301
ChainResidue
ATRP81
AHOH434
AHOH442
AASP184
ATRP186
ALYS187
AASP212
AASN213
AMG302
ASAM303
AHOH419

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AASP184
AASP212
AASN213
ADNC301
AHOH434

site_idAC3
Number of Residues21
Detailsbinding site for residue SAM A 303
ChainResidue
AMET83
AVAL85
AGLY109
AALA110
ATYR111
ATYR114
ASER115
AGLU133
AMET134
ATYR138
AGLY160
AALA161
ASER162
AGLN163
AASP184
AHIS185
ATRP186
ADNC301
AHOH450
AHOH498
AHOH564

site_idAC4
Number of Residues9
Detailsbinding site for residue DNC B 301
ChainResidue
BTRP81
BASP184
BLYS187
BASP212
BASN213
BMG302
BSAM303
BHOH443
BHOH446

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 302
ChainResidue
BASP184
BASP212
BASN213
BDNC301
BHOH443

site_idAC6
Number of Residues21
Detailsbinding site for residue SAM B 303
ChainResidue
BMET83
BVAL85
BGLY109
BALA110
BTYR111
BTYR114
BSER115
BGLU133
BMET134
BTYR138
BGLY160
BALA161
BSER162
BGLN163
BASP184
BHIS185
BTRP186
BDNC301
BHOH472
BHOH541
BHOH553

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12237326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01019","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

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

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

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PDB entries from 2025-12-24

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