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3VWD

Crystal structure of alpha-tubulin acetyltransferase domain of human Mec-17 in complex with acetoacetyl-CoA (P21212 form)

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 Residues34
DetailsBINDING SITE FOR RESIDUE ACO A 201
ChainResidue
ALYS56
AHIS133
AGLY134
AGLY136
AARG137
AASP157
AARG158
ASER160
ALYS162
ALYS165
APHE166
AGLN58
ALYS169
AHIS170
ACL202
AHOH301
AHOH307
AHOH308
AHOH312
AHOH338
AHOH346
AHOH349
AILE121
AHOH355
AHOH395
AHOH398
AHOH449
AHOH506
AASP123
APHE124
ATYR125
AILE126
AGLN131
AARG132

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 202
ChainResidue
AALA57
AGLU128
AGLN131
ALYS162
ALYS162
AACO201
AHOH303

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AARG69
AMET70
AHIS75
ALYS98

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 204
ChainResidue
AGLY188
APHE189
APHE190

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
AARG23
AVAL116
APHE189
APHE190
AHIS192
AGLN193
AHOH344
AHOH386

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23071314, ECO:0000269|PubMed:23071318, ECO:0000269|PubMed:24906155
ChainResidueDetails
APHE124
ASER160

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Crucial for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23071318
ChainResidueDetails
AGLN58

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-Rule:MF_03130
ChainResidueDetails
ALYS56
ALYS146

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PDB entries from 2024-07-24

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