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5GI7

Crystal Structure of Drosophila melanogaster Dopamine N-Acetyltransferase in Ternary Complex with CoA and Acetyl-phenylethylamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
Functional Information from PDB Data
site_idAC1
Number of Residues36
Detailsbinding site for residue COA A 301
ChainResidue
AASP46
AGLY154
ALEU155
AGLY156
AILE157
AALA158
ACYS181
ASER182
ASER186
ALYS192
A54W302
APRO48
AD1D304
AHOH417
AHOH427
AHOH436
AHOH448
AHOH460
AHOH465
AHOH468
AHOH471
AHOH494
AASP132
AHOH497
AHOH504
AHOH524
AHOH534
AHOH555
AHOH586
AHOH588
AVAL133
APRO135
ALEU146
ASER147
AVAL148
AARG153

site_idAC2
Number of Residues11
Detailsbinding site for residue 54W A 302
ChainResidue
APHE43
AGLU47
AASN50
AMET121
AGLY143
ALYS144
AILE145
ALEU146
AVAL179
ALEU180
ACOA301

site_idAC3
Number of Residues9
Detailsbinding site for residue 54W A 303
ChainResidue
ATHR41
APHE42
AGLU197
AARG200
AMET201
AVAL221
AGLY222
AILE223
AGLN224

site_idAC4
Number of Residues8
Detailsbinding site for residue D1D A 304
ChainResidue
APRO48
AHIS196
AGLU229
ACOA301
AHOH450
AHOH510
AHOH555
AHOH567

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22716280, ECO:0007744|PDB:3TE4
ChainResidueDetails
ALEU146
AGLY154

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Has a role in the catalytic activity => ECO:0000269|PubMed:25406072
ChainResidueDetails
ASER182
ASER186
AGLU47

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Might be involved in substrate binding => ECO:0000269|PubMed:25406072
ChainResidueDetails
ATYR64

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Regulates binding affinity for coenzyme A (CoASH) => ECO:0000269|PubMed:25406072
ChainResidueDetails
AARG153

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Acetyl-CoA => ECO:0000269|PubMed:22716280, ECO:0007744|PDB:3TE4
ChainResidueDetails
ALYS192

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PDB entries from 2024-05-01

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