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4UA3

Crystal structure of selenomethionine labeled SpNatD

Functional Information from GO Data
ChainGOidnamespacecontents
A0010485molecular_functionhistone H4 acetyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0043998molecular_functionhistone H2A acetyltransferase activity
B0010485molecular_functionhistone H4 acetyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0043998molecular_functionhistone H2A acetyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue COA A 301
ChainResidue
AILE120
ALYS133
AASN159
AASN161
AASN164
APHE165
ATYR166
AHIS168
APHE169
ACL302
AHOH470
AGLN121
AHOH476
AHOH524
BARG13
BLEU160
BASN164
BCOA301
ALEU122
AARG127
AGLY128
AARG129
AASN130
AVAL131
AGLY132

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AVAL155
APHE156
AASN159
ACOA301
BARG13

site_idAC3
Number of Residues30
Detailsbinding site for residue COA B 301
ChainResidue
AARG13
ALEU160
AASN161
AASN164
ACOA301
BILE120
BGLN121
BLEU122
BARG127
BGLY128
BARG129
BASN130
BVAL131
BGLY132
BLYS133
BASN159
BASN161
BALA162
BASN164
BPHE165
BTYR166
BHIS168
BPHE169
BHOH449
BHOH453
BHOH456
BHOH468
BHOH481
BHOH498
BHOH509

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q86UY6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25619998","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UA3","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Essential for catalytic activity","evidences":[{"source":"UniProtKB","id":"Q86UY6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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