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2IJA

Human N-acetyltransferase 1 F125S mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004060molecular_functionarylamine N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006805biological_processxenobiotic metabolic process
A0016407molecular_functionacetyltransferase activity
A0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
ATYR76
ATHR86
AHOH677
AHOH697
AHOH782

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACM A 301
ChainResidue
AHIS107
APHE217
APHE37
ATRP67
ACYS68
AILE106

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 502
ChainResidue
ATYR94
AARG187
ALYS188

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 503
ChainResidue
AHOH754

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 504
ChainResidue
APRO134
AGLN145
AHOH698

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 505
ChainResidue
AGLN133
AGLN145
AVAL146
AHOH686

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 506
ChainResidue
AGLU22

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 507
ChainResidue
AGLU22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate
ChainResidueDetails
ACYS68

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS107
AASP122

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR103
AGLY104
ATYR208
ASER214

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AILE106

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1e2t
ChainResidueDetails
ACYS68
AHIS107
AASP122

224201

PDB entries from 2024-08-28

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