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6WCD

Crystal Structure of Xenopus laevis APE2 Catalytic Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AASN9
AGLU34
AHOH515
AHOH517
AHOH561
AHOH657

site_idAC2
Number of Residues6
Detailsbinding site for residue MES A 402
ChainResidue
AGLU327
ALYS334
AHOH841
ALEU287
AASP288
APHE306

site_idAC3
Number of Residues9
Detailsbinding site for residue BU1 A 403
ChainResidue
AMET1
AASP28
ALEU41
ASER75
AGLN310
APRO311
AHOH521
AHOH544
AHOH631

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 404
ChainResidue
ALYS19
AGLU50
AGLY51

site_idAC5
Number of Residues7
Detailsbinding site for residue BU1 A 405
ChainResidue
AARG12
AALA13
AARG15
AHOH529
AHOH543
AHOH556
AHOH822

site_idAC6
Number of Residues7
Detailsbinding site for residue BU1 A 406
ChainResidue
AGLU107
AGLU108
ALYS157
AASN185
ATHR186
AASN205
AGLY207

Functional Information from PROSITE/UniProt
site_idPS00726
Number of Residues10
DetailsAP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. ADIICLQETK
ChainResidueDetails
AALA27-LYS36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P27695
ChainResidueDetails
ATYR142

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:32516598
ChainResidueDetails
AASP183

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
AHIS300

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:32516598, ECO:0007744|PDB:6WCD
ChainResidueDetails
AASN9

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764, ECO:0000269|PubMed:32516598, ECO:0007744|PDB:6WCD
ChainResidueDetails
AGLU34
AASP299

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
AASP183
AASN185
AHIS300

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P27695
ChainResidueDetails
AASN185

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P27695
ChainResidueDetails
AASP273

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Interaction with DNA substrate => ECO:0000250|UniProtKB:P27695
ChainResidueDetails
AHIS300

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PDB entries from 2024-05-01

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