Structure of PDB 2fcc Chain A

Receptor sequence
>2fccA (length=137) Species: 10665 (Tequatrovirus T4) [Search protein sequence]
TRINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFI
LGAGHVTFFYDKLEFLRKRQIELIAECLKRGFNIKDTTVQDISDIPQEFR
GDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
3D structure
PDB2fcc Structure of T4 Pyrimidine Dimer Glycosylase in a Reduced Imine Covalent Complex with Abasic Site-containing DNA.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T2
Catalytic site (residue number reindexed from 1) T1
Enzyme Commision number 3.2.2.17: deoxyribodipyrimidine endonucleosidase.
4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
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 dna A T2 R3 H16 E23 H34 G53 G55 V57 T58 Y61 R117 K121 R125 W128 T1 R2 H15 E22 H33 G52 G54 V56 T57 Y60 R116 K120 R124 W127
BS02 dna A M18 R22 R26 F83 N84 I85 K86 D87 M17 R21 R25 F82 N83 I84 K85 D86
Gene Ontology
Molecular Function
GO:0000704 pyrimidine dimer DNA N-glycosylase activity
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0004519 endonuclease activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016829 lyase activity
GO:0033959 deoxyribodipyrimidine endonucleosidase activity
GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Biological Process
GO:0006281 DNA repair

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2fcc, PDBe:2fcc, PDBj:2fcc
PDBsum2fcc
PubMed16916523
UniProtP04418|END5_BPT4 Endonuclease V

[Back to BioLiP]