Structure of PDB 4b5h Chain A

Receptor sequence
>4b5hA (length=259) Species: 487 (Neisseria meningitidis) [Search protein sequence]
MLKIISANVNGIRSAYKKGFYEYIAASGTDIVCVQELKAQEADLSADMKN
PHGMHGHWHCAEKRGYSGVAVYSKRKPDNVQIGMGIEEFDREGRFVRCDF
GRLSVISLYLPSGSSAEERQQVKYRFLDAFYPMLEAMKNEGRDIVVCGNW
NIAHQNIDLKNWKGNQKNSGFLPEEREWIGKVIHKLGWTDMWRTLYPDVP
GYTWWSNRGQAYAKDVGWRIDYQMVTPELAAKAVSAHVYKDEKFSDHAPL
VVEYDYAAE
3D structure
PDB4b5h Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.
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) N8 N10 E36 Y109 N149 N151 D221 D246 H247
Catalytic site (residue number reindexed from 1) N8 N10 E36 Y109 N149 N151 D221 D246 H247
Enzyme Commision number 3.1.11.2: exodeoxyribonuclease III.
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 S112 S114 S115 N165 N168 W204 Q210 W218 S112 S114 S115 N165 N168 W204 Q210 W218
BS02 dna A G11 R13 S14 K18 K38 R64 G65 N207 R208 G11 R13 S14 K18 K38 R64 G65 N207 R208
BS03 MN A N10 E36 N10 E36
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0004518 nuclease activity
GO:0008081 phosphoric diester hydrolase activity
GO:0008311 double-stranded DNA 3'-5' DNA exonuclease activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

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Molecular Function
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Biological Process
External links
PDB RCSB:4b5h, PDBe:4b5h, PDBj:4b5h
PDBsum4b5h
PubMed23035246
UniProtQ7DD47

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