Structure of PDB 7c3o Chain A

Receptor sequence
>7c3oA (length=316) Species: 237561 (Candida albicans SC5314) [Search protein sequence]
MLPPDILQNGEFETIYFQTNPTYIKSPIHIPKSTIGKPDTVKIRHFFALL
HQDLVVLGLEVFVYLQIYSDFVEKYVYVSKCDTVGLEKSTIKIGKVIGPV
LQYIINYNGYKIKMKNIEYRTLPKTQNLRLCVFTKPAKEYLFPNSAKNPY
KNLLNGQSLLRWWISIIDSITKGWNNHKLMIPGADKWATRKFIEKYSDWS
EGHIFKKDGLAVQAIPLFPDDPKGRFLELVIVECRYGKMTVSRFYQELAY
RQEFLLGDCVSLIGCCKENLEVTYHDDLVSTVTISEYKEFMNLLKLVDFS
DRVEVSNFVSNYRKSK
3D structure
PDB7c3o Crystal structure of TT109 from CANDIDA ALBICANS
ChainA
Resolution1.89 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.48: histone acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ACO A C81 D82 T83 K92 I93 F176 K178 A180 Y183 N195 L197 L202 C81 D82 T83 K92 I93 F133 K135 A137 Y140 N152 L154 L159
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
GO:0010484 histone H3 acetyltransferase activity
GO:0016740 transferase activity
GO:0032931 histone H3K56 acetyltransferase activity
Biological Process
GO:0006289 nucleotide-excision repair
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0006355 regulation of DNA-templated transcription
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
GO:0006896 Golgi to vacuole transport
GO:0006974 DNA damage response
GO:0030447 filamentous growth
GO:0036166 phenotypic switching
GO:0044182 filamentous growth of a population of unicellular organisms
GO:1900239 regulation of phenotypic switching
GO:1900429 negative regulation of filamentous growth of a population of unicellular organisms
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7c3o, PDBe:7c3o, PDBj:7c3o
PDBsum7c3o
PubMed
UniProtQ5AAJ8|RT109_CANAL Histone acetyltransferase RTT109 (Gene Name=RTT109)

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