eF-site ID 1bix-A PDB Code 1bix Chain A click to enlarge Title THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES Classification DNA REPAIR Compound AP ENDONUCLEASE 1 Source null (APEX1_HUMAN) Sequence A:  LYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDW VKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPS DKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFD SFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRK PLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGEL LQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLD YFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Description Functional site 1) chain A residue 65 type sequence C description CYS 65 HAS BEEN PROPOSED TO BE INVOLVED IN THE REDUCTIVE ACTIVATION OF A NUMBER OF TRANSCRIPTION FACTORS INCLUDING FOS/JUN AND P53. source : ROX 2) chain A residue 216 type sequence E description BINDING SITE FOR RESIDUE SM A 400 source : AC1 3) chain A residue 217 type sequence E description BINDING SITE FOR RESIDUE SM A 400 source : AC1 4) chain A residue 242 type sequence E description BINDING SITE FOR RESIDUE SM A 400 source : AC1 5) chain A residue 245 type sequence Q description BINDING SITE FOR RESIDUE SM A 400 source : AC1 6) chain A residue 70 type sequence D description BINDING SITE FOR RESIDUE SM A 401 source : AC2 7) chain A residue 96 type sequence E description BINDING SITE FOR RESIDUE SM A 401 source : AC2 8) chain A residue 46 type sequence E description BINDING SITE FOR RESIDUE SM A 402 source : AC3 9) chain A residue 148 type sequence D description BINDING SITE FOR RESIDUE SM A 402 source : AC3 10) chain A residue 150 type sequence E description BINDING SITE FOR RESIDUE SM A 402 source : AC3 11) chain A residue 124 type sequence D description BINDING SITE FOR RESIDUE SM A 403 source : AC4 12) chain A residue 126 type sequence E description BINDING SITE FOR RESIDUE SM A 403 source : AC4 13) chain A residue 318 type sequence L description BINDING SITE FOR RESIDUE SM A 403 source : AC4 14) chain A residue 271 type sequence M description BINDING SITE FOR RESIDUE PT A 404 source : AC5 15) chain A residue 276 type sequence K description BINDING SITE FOR RESIDUE PT A 404 source : AC5 16) chain A residue 71 type catalytic sequence G description 510 source MCSA : MCSA1 17) chain A residue 97 type catalytic sequence T description 510 source MCSA : MCSA1 18) chain A residue 172 type catalytic sequence V description 510 source MCSA : MCSA1 19) chain A residue 211 type catalytic sequence L description 510 source MCSA : MCSA1 20) chain A residue 213 type catalytic sequence V description 510 source MCSA : MCSA1 21) chain A residue 284 type catalytic sequence Y description 510 source MCSA : MCSA1 22) chain A residue 309 type catalytic sequence H description 510 source MCSA : MCSA1 23) chain A residue 310 type catalytic sequence C description 510 source MCSA : MCSA1 24) chain A residue 311 type MOD_RES sequence P description S-nitrosocysteine => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI14 25) chain A residue 55 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 26) chain A residue 94 type MOD_RES sequence L description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI11 27) chain A residue 66 type MOD_RES sequence S description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI11 28) chain A residue 198 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI12 29) chain A residue 234 type MOD_RES sequence P description Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352 source Swiss-Prot : SWS_FT_FI13 30) chain A residue 89-98 type prosite sequence PDILCLQETK description AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK source prosite : PS00726 31) chain A residue 251-267 type prosite sequence DSFRHLYPNTPYAYTFW description AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW source prosite : PS00727 32) chain A residue 277-288 type prosite sequence NVGWRLDYFLLS description AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS source prosite : PS00728 33) chain A residue 97 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 211 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 213 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 309 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 310 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 69 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 213 type SITE sequence V description Transition state stabilizer => ECO:0000269|PubMed:8932375 source Swiss-Prot : SWS_FT_FI6 40) chain A 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 41) chain A residue 310 type SITE sequence C description Interaction with DNA substrate source Swiss-Prot : SWS_FT_FI8 42) chain A residue 172 type ACT_SITE sequence V description ACT_SITE => ECO:0000269|PubMed:15380100 source Swiss-Prot : SWS_FT_FI1 43) chain A 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 44) chain A residue 310 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI3

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