Structure of PDB 6tc9 Chain A

Receptor sequence
>6tc9A (length=259) Species: 996307 (Neisseria meningitidis alpha522) [Search protein sequence]
PELPEVETTLRGIAPHIEGKTVEAVVLRQLLRWQINPDLGEILSGRQVLS
CGRRAKYLLIRFQTGVLLIHLGMSGSLRIFTPSDGRIGRPDRHDHVDIVF
SDGTVMRYRDPRKFGAILWYEGIEEHHPLLEKLGPEPLSEAFCADYLYAR
LKAQKRAVKLALMDNAVVVGVGNIYANESLFRAGISPHRPANRLKKKECA
LLVETVKAVLQRAIETGGYFQQEYTVYGRHNQPCPRCGGLVVKETLGQRG
TFYCPNCQK
3D structure
PDB6tc9 Conformational changes of DNA repair glycosylase MutM triggered by DNA binding.
ChainA
Resolution2.175 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 P2 E3 R34 W35 K58 H72 G74 M75 R114 F116 L131 N175 I176 Y243 K259 R265 P1 E2 R32 W33 K56 H70 G72 M73 R112 F114 L129 N173 I174 Y227 K243 R249
BS02 dna A R94 H95 P113 R114 K115 F116 R92 H93 P111 R112 K113 F114
BS03 ZN A C250 C253 C270 C273 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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6tc9, PDBe:6tc9, PDBj:6tc9
PDBsum6tc9
PubMed32598485
UniProtI4E596

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