Structure of PDB 1l1t Chain A

Receptor sequence
>1l1tA (length=259) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
PELPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDQTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSFQHHLYVYGRQGNPCKRCGTPIEKTVVAGRG
THYCPRCQR
3D structure
PDB1l1t Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.2.23: DNA-formamidopyrimidine glycosylase.
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 H93 V111 R112 K113 F114 H92 V110 R111 K112 F113
BS02 dna A E3 K60 H74 R76 M77 R112 F114 G173 N174 I175 Y242 K258 R264 E2 K59 H73 R75 M76 R111 F113 G172 N173 I174 Y227 K243 R249
BS03 ZN A C249 C252 C269 C272 C234 C237 C254 C257
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003684 damaged DNA binding
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0008270 zinc ion binding
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0016829 lyase activity
GO:0019104 DNA N-glycosylase activity
GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
GO:0046872 metal ion binding
GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1l1t, PDBe:1l1t, PDBj:1l1t
PDBsum1l1t
PubMed12055620
UniProtP84131

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