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5K05

Crystal Structure of COMT in complex with 4-methyl-2-(4-methylphenyl)-5-(1H-pyrazol-5-yl)-1,3-thiazole

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 Residues12
Detailsbinding site for residue 6P5 A 301
ChainResidue
AGLY66
ATRP143
AARG146
BARG78
ATYR68
AMET89
AGLU90
AILE91
AALA118
ASER119
AGLN120
AHIS142

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
APRO82
AGLY83
AARG85
ALYS111

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG8
ATYR32
ALYS36

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG8
ATRP38

site_idAC5
Number of Residues12
Detailsbinding site for residue 6P5 B 301
ChainResidue
AARG78
BGLY66
BTYR68
BMET89
BGLU90
BILE91
BSER119
BGLN120
BHIS142
BTRP143
BARG146
BHOH417

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 302
ChainResidue
BARG8
BTYR32
BLYS36

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 B 303
ChainResidue
AARG11
BSER195
BSER196
BTYR197

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 B 304
ChainResidue
BTHR4
BLYS5
BHOH401

site_idAC9
Number of Residues2
Detailsbinding site for residue SO4 B 305
ChainResidue
BARG8
BTRP38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
BASP3-PRO19
AASP3-PRO19

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:12237326
ChainResidueDetails
BASP133
BARG184
AARG85
ALEU115
AASP133
AARG184
BARG85
BLEU115

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01019
ChainResidueDetails
ALYS162
BGLY107
BTHR134
BLYS162
AGLY107
ATHR134

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATYR212
AGLN213
BLEU160
BSER187
BTYR212
BGLN213
ALEU160
ASER187

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 915
ChainResidueDetails
AARG184metal ligand
ASER187proton shuttle (general acid/base)
ATYR212metal ligand
AGLN213metal ligand

site_idMCSA2
Number of Residues4
DetailsM-CSA 915
ChainResidueDetails
BARG184metal ligand
BSER187proton shuttle (general acid/base)
BTYR212metal ligand
BGLN213metal ligand

221051

PDB entries from 2024-06-12

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