Structure of PDB 1q2d Chain A

Receptor sequence
>1q2dA (length=161) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
LDFDILTNDGTHRNMKLLIDLKNIFSRQLPKMPKEYIVKLVFDRHHESMV
ILKNKQKVIGGICFRQYKPQRFAEVAFLAVTANEQVRGYGTRLMNKFKDH
MQKQNIEYLLTYADNFAIGYFKKQGFTKEHRMPQEKWKGYIKDYDGGTLM
ECYIHPYVDYG
3D structure
PDB1q2d Molecular basis for GCN5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y115 F120 E122 V123 A124 L126 L158 I189 Y192
Catalytic site (residue number reindexed from 1) Y67 F72 E74 V75 A76 L78 L110 I141 Y144
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 peptide A L77 P78 K79 A124 F125 L126 T159 Y160 D162 N163 F164 A165 F169 L29 P30 K31 A76 F77 L78 T111 Y112 D114 N115 F116 A117 F121
BS02 COA A Q76 L77 L126 A127 V128 Q133 V134 G136 G138 T139 F164 Q28 L29 L78 A79 V80 Q85 V86 G88 G90 T91 F116
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups

View graph for
Molecular Function
External links
PDB RCSB:1q2d, PDBe:1q2d, PDBj:1q2d
PDBsum1q2d
PubMed14661947
UniProtQ27198

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