eF-site ID 3d6n-AB PDB Code 3d6n Chain A, B click to enlarge Title Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase Classification HYDROLASE/TRANSFERASE Compound Dihydroorotase Source Aquifex aeolicus (PYRB_AQUAE) Sequence A:  MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILV PEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSR CAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCR VLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDS SVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALL GLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLE IIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPP LRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFA MPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARII GVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPL WGKVLKGKVIYTIKDGKMVYKD B:  MRSLISSLDLTREEVEEILKYAKEFKEGKEETIKASAVLF FSEPSTRTRLSFEKAARELGIETYLVSGSESSTVKGESFF DTLKTFEGLGFDYVVFRVPFVFFPYKEIVKSLNLRLVNAG DGTHQHPSQGLIDFFTIKEHFGEVKDLRVLYVGDIKHSRV FRSGAPLLNMFGAKIGVCGPKTLIPRDVEVFKVDVFDDVD KGIDWADVVIWLRLQKERQKENYIPSESSYFKQFGLTKER FEKVKLYMHPGPVNRNVDIDHELVYTEKSLIQEQVKNGIP VRKAIYKFLWT Description Functional site 1) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE ZN A 423 source : AC1 2) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE ZN A 423 source : AC1 3) chain A residue 153 type sequence D description BINDING SITE FOR RESIDUE ZN A 423 source : AC1 4) chain A residue 305 type sequence D description BINDING SITE FOR RESIDUE ZN A 423 source : AC1 5) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 6) chain A residue 65 type sequence R description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 7) chain A residue 95 type sequence N description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 8) chain A residue 153 type sequence D description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 9) chain A residue 154 type sequence G description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 10) chain A residue 180 type sequence H description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 11) chain A residue 232 type sequence H description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 12) chain A residue 278 type sequence N description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 13) chain A residue 305 type sequence D description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 14) chain A residue 307 type sequence A description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 15) chain A residue 309 type sequence H description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 16) chain A residue 322 type sequence P description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 17) chain A residue 323 type sequence G description BINDING SITE FOR RESIDUE FLC A 424 source : AC2 18) chain B residue 48 type sequence T description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 19) chain B residue 97 type sequence R description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 20) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 21) chain B residue 159 type sequence R description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 22) chain B residue 213 type sequence R description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 23) chain B residue 251 type sequence G description BINDING SITE FOR RESIDUE FLC B 292 source : AC3 24) chain B residue 41-48 type prosite sequence FSEPSTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FsEpSTRT source prosite : PS00097 25) chain A residue 59-67 type prosite sequence DIHVHLRDP description DIHYDROOROTASE_1 Dihydroorotase signature 1. DIHVHLRdP source prosite : PS00482 26) chain A residue 303-314 type prosite sequence ATDHAPHQTFEK description DIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHqtfeK source prosite : PS00483 27) chain B residue 47 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 252 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 48 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 75 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 97 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 126 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 129 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 159 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 213 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 251 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 61 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI2 38) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI2 39) chain A residue 153 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI2 40) chain A residue 95 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI3 41) chain A residue 278 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI3 42) chain A residue 309 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI3 43) chain A residue 322 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI3 44) chain A residue 305 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH source Swiss-Prot : SWS_FT_FI4

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