eF-site ID 1hd7-A PDB Code 1hd7 Chain A click to enlarge Title A Second Divalent Metal Ion in the Active Site of a New Crystal Form of Human Apurinic/Apyridinimic Endonuclease, Ape1, and its Implications for the Catalytic Mechanism Classification DNA REPAIR Compound DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE Source Homo sapiens (Human) (APE1_HUMAN) Sequence A:  LYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDW VKEEAPDILCLQETKCSEGLSHQYWSAPYSGVGLLSRQCP LKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGL VRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEID LRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPN TPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSK IRSKALGSDHCPITLYLAL Description 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 71 type catalytic sequence G description 510 source MCSA : MCSA1 4) chain A residue 97 type catalytic sequence T description 510 source MCSA : MCSA1 5) chain A residue 172 type catalytic sequence V description 510 source MCSA : MCSA1 6) chain A residue 211 type catalytic sequence L description 510 source MCSA : MCSA1 7) chain A residue 213 type catalytic sequence V description 510 source MCSA : MCSA1 8) chain A residue 284 type catalytic sequence Y description 510 source MCSA : MCSA1 9) chain A residue 309 type catalytic sequence H description 510 source MCSA : MCSA1 10) chain A residue 310 type catalytic sequence C description 510 source MCSA : MCSA1 11) chain A residue 89-98 type prosite sequence PDILCLQETK description AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK source prosite : PS00726 12) chain A residue 251-267 type prosite sequence DSFRHLYPNTPYAYTFW description AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW source prosite : PS00727 13) chain A residue 277-288 type prosite sequence NVGWRLDYFLLS description AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS source prosite : PS00728 14) chain A residue 172 type ACT_SITE sequence V description ACT_SITE => ECO:0000269|PubMed:15380100 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 55 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 16) chain A residue 66 type MOD_RES sequence S description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 17) chain A residue 94 type MOD_RES sequence L description S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI12 18) chain A residue 198 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 19) chain A residue 234 type MOD_RES sequence P description Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352 source Swiss-Prot : SWS_FT_FI14 20) chain A residue 311 type MOD_RES sequence P description S-nitrosocysteine => ECO:0000269|PubMed:17403694 source Swiss-Prot : SWS_FT_FI15 21) 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 22) chain A residue 310 type ACT_SITE sequence C description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 69 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 97 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 211 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 213 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 309 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 310 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00764 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 213 type SITE sequence V description Transition state stabilizer => ECO:0000269|PubMed:8932375 source Swiss-Prot : SWS_FT_FI6 30) 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 31) chain A residue 310 type SITE sequence C description Interaction with DNA substrate source Swiss-Prot : SWS_FT_FI8

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