eF-site ID 1lwv-ADE PDB Code 1lwv Chain A, D, E click to enlarge Title Borohydride-trapped hOgg1 Intermediate Structure Co-Crystallized with 8-aminoguanine Classification HYDROLASE/DNA Compound 5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3' Source null (1LWV) Sequence A:  GSEGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWR EQSPAHWSGVLADQVWTLTQTEEQLHCTVYRSQASRPTPD ELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVR LLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLI QLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSAS ARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVA DCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGP SPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQ D:  GGTAGACCTGGACGC E:  GCGTCCAXGTCTACC Description (1)  8-OXOGUANINE DNA GLYCOSYLASE (E.C.3.2.2.-)/DNA Complex Functional site 1) chain E residue 22 type sequence A description BINDING SITE FOR RESIDUE CA E 153 source : AC1 2) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 3) chain A residue 45 type sequence F description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 4) chain A residue 144 type sequence F description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 5) chain A residue 249 type sequence K description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 6) chain A residue 257 type sequence M description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 7) chain A residue 266 type sequence P description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 8) chain A residue 268 type sequence D description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 9) chain A residue 271 type sequence M description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 10) chain A residue 315 type sequence Q description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 11) chain A residue 319 type sequence F description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 12) chain E residue 23 type sequence X description BINDING SITE FOR RESIDUE ANG A 328 source : AC2 13) chain A residue 249 type ACT_SITE sequence K description Schiff-base intermediate with DNA => ECO:0000269|PubMed:9197244 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 149 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 154 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 204 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 270 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 287 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10706276, ECO:0000269|PubMed:11902834, ECO:0000269|PubMed:12578369, ECO:0000269|PubMed:12592398, ECO:0000269|PubMed:15610848 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 266 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 268 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 315 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 319 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 249 type catalytic sequence K description 185 source MCSA : MCSA1 24) chain A residue 268 type catalytic sequence D description 185 source MCSA : MCSA1

Display surface Download Links