eF-site ID 1e9n-B PDB Code 1e9n Chain B 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 B:  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 B residue 210 type sequence D description BINDING SITE FOR RESIDUE PB B1319 source : AC3 2) chain B residue 212 type sequence N description BINDING SITE FOR RESIDUE PB B1319 source : AC3 3) chain B residue 282 type sequence L description BINDING SITE FOR RESIDUE PB B1319 source : AC3 4) chain B residue 309 type sequence H description BINDING SITE FOR RESIDUE PB B1319 source : AC3 5) chain B residue 96 type sequence E description BINDING SITE FOR RESIDUE PB B1320 source : AC4 6) chain B residue 71 type catalytic sequence G description 510 source MCSA : MCSA2 7) chain B residue 97 type catalytic sequence T description 510 source MCSA : MCSA2 8) chain B residue 172 type catalytic sequence V description 510 source MCSA : MCSA2 9) chain B residue 211 type catalytic sequence L description 510 source MCSA : MCSA2 10) chain B residue 213 type catalytic sequence V description 510 source MCSA : MCSA2 11) chain B residue 284 type catalytic sequence Y description 510 source MCSA : MCSA2 12) chain B residue 309 type catalytic sequence H description 510 source MCSA : MCSA2 13) chain B residue 310 type catalytic sequence C description 510 source MCSA : MCSA2 14) chain B residue 311 type MOD_RES sequence P description S-nitrosocysteine => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI15 15) chain B residue 310 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 69 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 17) chain B residue 97 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 211 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 213 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 309 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 310 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 55 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 23) chain B residue 66 type MOD_RES sequence S description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 24) chain B residue 94 type MOD_RES sequence L description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 25) chain B residue 198 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 26) chain B residue 234 type MOD_RES sequence P description Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352 source Swiss-Prot : SWS_FT_FI14 27) chain B residue 172 type ACT_SITE sequence V description ACT_SITE => ECO:0000269|PubMed:15380100 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 211 type ACT_SITE sequence L description Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX source Swiss-Prot : SWS_FT_FI2 29) chain B residue 213 type SITE sequence V description Transition state stabilizer => ECO:0000269|PubMed:8932375 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 284 type SITE sequence Y description Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799 source Swiss-Prot : SWS_FT_FI7 31) chain B residue 310 type SITE sequence C description Interaction with DNA substrate source Swiss-Prot : SWS_FT_FI8

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