eF-site ID 1e9n-A PDB Code 1e9n Chain A click to enlarge Title A second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism Classification DNA REPAIR Compound DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE Source (APE1_HUMAN) Sequence A:  ALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLD WVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAP SEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDS FVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKP LVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELL QAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDY FLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Description (1)  DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE (E.C.4.2.99.18) Functional site 1) chain A residue 70 type sequence D description BINDING SITE FOR RESIDUE PB A1319 source : AC1 2) chain A residue 96 type sequence E description BINDING SITE FOR RESIDUE PB A1319 source : AC1 3) chain A residue 210 type sequence D description BINDING SITE FOR RESIDUE PB A1320 source : AC2 4) chain A residue 212 type sequence N description BINDING SITE FOR RESIDUE PB A1320 source : AC2 5) chain A residue 309 type sequence H description BINDING SITE FOR RESIDUE PB A1320 source : AC2 6) chain A residue 70 type catalytic sequence D description 510 source MCSA : MCSA1 7) chain A residue 96 type catalytic sequence E description 510 source MCSA : MCSA1 8) chain A residue 171 type catalytic sequence Y description 510 source MCSA : MCSA1 9) chain A residue 210 type catalytic sequence D description 510 source MCSA : MCSA1 10) chain A residue 212 type catalytic sequence N description 510 source MCSA : MCSA1 11) chain A residue 283 type catalytic sequence D description 510 source MCSA : MCSA1 12) chain A residue 308 type catalytic sequence D description 510 source MCSA : MCSA1 13) chain A residue 309 type catalytic sequence H description 510 source MCSA : MCSA1 14) chain A residue 89-98 type prosite sequence PDILCLQETK description AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK source prosite : PS00726 15) chain A residue 251-267 type prosite sequence DSFRHLYPNTPYAYTFW description AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW source prosite : PS00727 16) chain A residue 277-288 type prosite sequence NVGWRLDYFLLS description AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS source prosite : PS00728 17) chain A residue 310 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI15 18) chain A residue 283 type SITE sequence D description Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 309 type SITE sequence H description Interaction with DNA substrate source Swiss-Prot : SWS_FT_FI8 20) chain A residue 54 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 21) chain A residue 171 type ACT_SITE sequence Y description ACT_SITE => ECO:0000269|PubMed:15380100 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 210 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX source Swiss-Prot : SWS_FT_FI2 23) chain A residue 309 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 68 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 96 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 210 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 308 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 309 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 212 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:8932375 source Swiss-Prot : SWS_FT_FI6 31) chain A residue 65 type MOD_RES sequence C description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 32) chain A residue 93 type MOD_RES sequence C description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 33) chain A residue 197 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 34) chain A residue 233 type MOD_RES sequence T description Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352 source Swiss-Prot : SWS_FT_FI14

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