Structure of PDB 5wn2 Chain A

Receptor sequence
>5wn2A (length=276) Species: 9606 (Homo sapiens) [Search protein sequence]
ALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDIL
CLQQTKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQAPLKV
SYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAF
RKFLKGLASRKPLVLCGNLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGE
LLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLL
PALCDSKIRSKALGSDHCPITLYLAL
3D structure
PDB5wn2 Molecular snapshots of APE1 proofreading mismatches and removing DNA damage.
ChainA
Resolution2.288 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N68 Q96 N210 N212 D283 D308 H309
Catalytic site (residue number reindexed from 1) N26 Q54 N168 N170 D241 D266 H267
Enzyme Commision number 3.1.11.2: exodeoxyribonuclease III.
3.1.21.-
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 N222 M271 K276 W280 N180 M229 K234 W238
BS02 dna A Y128 Y171 R177 Y86 Y129 R135
BS03 dna A G71 R73 A74 K78 K98 Y269 M270 G29 R31 A32 K36 K56 Y227 M228
BS04 PGA A Q96 Y171 N174 N212 F266 Q54 Y129 N132 N170 F224
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003824 catalytic activity
GO:0004518 nuclease activity
GO:0004519 endonuclease activity
Biological Process
GO:0006281 DNA repair

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Molecular Function
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Biological Process
External links
PDB RCSB:5wn2, PDBe:5wn2, PDBj:5wn2
PDBsum5wn2
PubMed29374164
UniProtP27695|APEX1_HUMAN DNA repair nuclease/redox regulator APEX1 (Gene Name=APEX1)

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