eF-site ID 1hu0-A PDB Code 1hu0 Chain A click to enlarge Title CRYSTAL STRUCTURE OF AN HOGG1-DNA BOROHYDRIDE TRAPPED INTERMEDIATE COMPLEX Classification HYDROLASE/DNA Compound 5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3' Source Homo sapiens (Human) (1HU0) Sequence A:  GSEGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWR EQSPAHWSGVLADQVWTLTQTEEQLHCTVYRSQASRPTPD ELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVR LLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLI QLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSAS ARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVA DCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGP SPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQ Description Functional site 1) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 2) chain A residue 45 type sequence F description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 3) chain A residue 144 type sequence F description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 4) chain A residue 249 type sequence K description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 5) chain A residue 266 type sequence P description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 6) chain A residue 268 type sequence D description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 7) chain A residue 315 type sequence Q description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 8) chain A residue 319 type sequence F description BINDING SITE FOR RESIDUE OXG A 328 source : AC2 9) chain A residue 249 type catalytic sequence K description 185 source MCSA : MCSA1 10) chain A residue 268 type catalytic sequence D description 185 source MCSA : MCSA1 11) 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 12) 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 13) 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 14) 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 15) 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 16) 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 17) chain A residue 266 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 268 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 315 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 319 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI3

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