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5P94

humanized rat catechol O-methyltransferase in complex with 5-(4-fluorophenyl)-2,3-dihydroxy-N-[[3-[(1H-indazol-5-ylamino)methyl]phenyl]methyl]benzamide at 1.20A

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 Residues5
Detailsbinding site for residue MG A 301
ChainResidue
AASP141
AASP169
AASN170
A76T306
AHOH421

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AHOH445
AASN41
AVAL42
ATYR71
ASER72

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
AASP44
AALA45
ATYR200
AHOH567

site_idAC4
Number of Residues10
Detailsbinding site for residue NHE A 304
ChainResidue
AGLU37
ATRP38
AGLN100
AILE114
ALEU115
ATYR130
AMET201
A76T306
AHOH549
AHOH559

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 305
ChainResidue
AGLY83
AARG85
ALYS111
ALYS128

site_idAC6
Number of Residues23
Detailsbinding site for residue 76T A 306
ChainResidue
AMET40
AMET89
AGLU90
AILE91
AALA97
AGLN100
AGLN101
ASER119
AASP141
AHIS142
ATRP143
ALYS144
AASP169
AASN170
AGLU199
AMG301
ANHE304
AHOH421
AHOH442
AHOH497
AHOH502
AHOH514
AHOH544

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 A 307
ChainResidue
AASP3
ATHR4
ALYS5
AARG8
AHOH422
AHOH460
AHOH475

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
AILE91
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_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 2024-07-24

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