Structure of PDB 4ejz Chain A

Receptor sequence
>4ejzA (length=289) Species: 273068 (Caldanaerobacter subterraneus subsp. tengcongensis MB4) [Search protein sequence]
MKYNVEEKGTKVIVRGIADFNLKETFESGQCFRWNEEEDGSYTGVAYDRV
VNVKLEGDTLIIDNTNLTDFYDIWFDYFDLGRDYGQIKESLSKDPVLKEA
IKFGQGIRILRQDTWETLVSFIVSQNNRIPQIKKVIENLATSFGNPIEYK
GKIYYTFPKPEELVMYDVETIAKTRCGFRAKYIFDAASKVFSGEINLLKL
HEYSTSEIRDILMTINGVGPKVADCVILYSIGRYDTFPTDVWIKRIVEHL
YLKREGTPVEIQLFAIDKFGDLSGFAQQYLFYYGREMGK
3D structure
PDB4ejz Crystal structures of MBOgg1 in complex with two abasic DNA ligands
ChainA
Resolution3.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K221 D240
Catalytic site (residue number reindexed from 1) K221 D240
Enzyme Commision number 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 Q125 N126 R128 F178 N216 G217 V218 G219 P220 K221 V222 D240 V241 W242 Q125 N126 R128 F178 N216 G217 V218 G219 P220 K221 V222 D240 V241 W242 PDBbind-CN: Kd=8.2nM
BS02 dna A R175 G177 F178 R179 R175 G177 F178 R179 PDBbind-CN: Kd=8.2nM
Gene Ontology
Molecular Function
GO:0003684 damaged DNA binding
GO:0003824 catalytic activity
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0140097 catalytic activity, acting on DNA
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006289 nucleotide-excision repair

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Molecular Function
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Biological Process
External links
PDB RCSB:4ejz, PDBe:4ejz, PDBj:4ejz
PDBsum4ejz
PubMed23246782
UniProtQ8R5T9

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