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4PK2

tubulin acetyltransferase complex with bisubstrate analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0005874cellular_componentmicrotubule
A0019799molecular_functiontubulin N-acetyltransferase activity
A0071929biological_processalpha-tubulin acetylation
Functional Information from PDB Data
site_idAC1
Number of Residues47
Detailsbinding site for B 1 to 7, bisubstrate analog
ChainResidue
AGLN58
APHE124
ATYR125
AILE126
AGLN131
AARG132
AHIS133
AGLY134
AGLY136
AARG137
AASP157
AILE64
AARG158
ASER160
ALYS162
ALEU163
ALYS165
APHE166
ALYS169
AHIS170
AASN182
APHE183
ASER83
AHOH303
AHOH323
AHOH332
AHOH340
AHOH358
AHOH379
AHOH386
AHOH393
AHOH395
AHOH396
ASER84
AHOH521
AHOH525
AHOH547
BHOH101
BHOH102
BHOH103
BHOH105
BHOH106
AALA85
AARG86
ALYS102
ALEU122
AASP123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071314","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23071318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24906155","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Crucial for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071318","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q8K341","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03130","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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