eF-site ID 4c6c-A PDB Code 4c6c Chain A click to enlarge Title Crystal structure of the dihydroorotase domain of human CAD in apo- form obtained recombinantly from HEK293 cells. Classification HYDROLASE Compound CAD PROTEIN Source Homo sapiens (Human) (PYR1_HUMAN) Sequence A:  KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITM VCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS ENAGTLGTVAGSAAGLXLYLNETFSELRLDSVVQWMEHFE TWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGE VRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRI FHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV KGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQ LP Description Functional site 1) chain A residue 1471 type sequence H description BINDING SITE FOR RESIDUE ZN A 2822 source : AC1 2) chain A residue 1473 type sequence H description BINDING SITE FOR RESIDUE ZN A 2822 source : AC1 3) chain A residue 1556 type sequence X description BINDING SITE FOR RESIDUE ZN A 2822 source : AC1 4) chain A residue 1686 type sequence D description BINDING SITE FOR RESIDUE ZN A 2822 source : AC1 5) chain A residue 1556 type sequence X description BINDING SITE FOR RESIDUE ZN A 2823 source : AC2 6) chain A residue 1590 type sequence H description BINDING SITE FOR RESIDUE ZN A 2823 source : AC2 7) chain A residue 1614 type sequence H description BINDING SITE FOR RESIDUE ZN A 2823 source : AC2 8) chain A residue 1471 type sequence H description BINDING SITE FOR RESIDUE ZN A 2824 source : AC3 9) chain A residue 1613 type sequence C description BINDING SITE FOR RESIDUE ZN A 2824 source : AC3 10) chain A residue 1637 type sequence E description BINDING SITE FOR RESIDUE ZN A 2824 source : AC3 11) chain A residue 1734 type sequence H description BINDING SITE FOR RESIDUE ZN A 2825 source : AC4 12) chain A residue 1741 type sequence H description BINDING SITE FOR RESIDUE ZN A 2825 source : AC4 13) chain A residue 1586 type sequence P description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 14) chain A residue 1587 type sequence I description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 15) chain A residue 1608 type sequence R description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 16) chain A residue 1609 type sequence S description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 17) chain A residue 1610 type sequence V description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 18) chain A residue 1611 type sequence H description BINDING SITE FOR RESIDUE FMT A 2826 source : AC5 19) chain A residue 1734 type sequence H description BINDING SITE FOR RESIDUE FMT A 2827 source : AC6 20) chain A residue 1734 type sequence H description BINDING SITE FOR RESIDUE FMT A 2827 source : AC6 21) chain A residue 1737 type sequence R description BINDING SITE FOR RESIDUE FMT A 2827 source : AC6 22) chain A residue 1737 type sequence R description BINDING SITE FOR RESIDUE FMT A 2827 source : AC6 23) chain A residue 1463 type sequence R description BINDING SITE FOR RESIDUE FMT A 2828 source : AC7 24) chain A residue 1748 type sequence T description BINDING SITE FOR RESIDUE FMT A 2828 source : AC7 25) chain A residue 1473 type sequence H description BINDING SITE FOR RESIDUE FMT A 2829 source : AC8 26) chain A residue 1475 type sequence R description BINDING SITE FOR RESIDUE FMT A 2829 source : AC8 27) chain A residue 1505 type sequence N description BINDING SITE FOR RESIDUE FMT A 2829 source : AC8 28) chain A residue 1690 type sequence H description BINDING SITE FOR RESIDUE FMT A 2829 source : AC8 29) chain A residue 1702 type sequence P description BINDING SITE FOR RESIDUE FMT A 2829 source : AC8 30) chain A residue 1469-1477 type prosite sequence DVHVHLREP description DIHYDROOROTASE_1 Dihydroorotase signature 1. DVHVHLReP source prosite : PS00482 31) chain A residue 1684-1695 type prosite sequence ASDHAPHTLEEK description DIHYDROOROTASE_2 Dihydroorotase signature 2. ASDhAPHtleeK source prosite : PS00483 32) chain A residue 1556 type MOD_RES sequence X description N6-carboxylysine => ECO:0000269|PubMed:24332717 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 1505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q source Swiss-Prot : SWS_FT_FI3 34) chain A residue 1661 type BINDING sequence R description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q source Swiss-Prot : SWS_FT_FI3 35) chain A residue 1690 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q source Swiss-Prot : SWS_FT_FI3 36) chain A residue 1702 type BINDING sequence P description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q source Swiss-Prot : SWS_FT_FI3 37) chain A residue 1475 type BINDING sequence R description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6Q source Swiss-Prot : SWS_FT_FI3 38) chain A residue 1686 type ACT_SITE sequence D description For DHOase activity => ECO:0000250|UniProtKB:P05020 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 1614 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 40) chain A residue 1637 type BINDING sequence E description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 41) chain A residue 1686 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 42) chain A residue 1471 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 43) chain A residue 1473 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 44) chain A residue 1590 type BINDING sequence H description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 45) chain A residue 1613 type BINDING sequence C description BINDING => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI2 46) chain A residue 1556 type BINDING sequence X description via carbamate group => ECO:0000269|PubMed:24332717, ECO:0007744|PDB:4C6D source Swiss-Prot : SWS_FT_FI4

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