eF-site ID 4bjh-A PDB Code 4bjh Chain A click to enlarge Title Crystal Structure of the Aquifex Reactor Complex Formed by Dihydroorotase (H180A, H232A) with Dihydroorotate and Aspartate Transcarbamoylase with N-(phosphonacetyl)-L-aspartate (PALA) Classification HYDROLASE/TRANSFERASE Compound DIHYDROOROTASE Source (PYRB_AQUAE) Sequence A:  MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILV PEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSR CAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCR VLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDS SVMRKALELASQLGVPIMDACEDDKLAYGVINEGEVSALL GLSSRAPEAEEIQIARDGILAQRTGGHVHIQAVSTKLSLE IIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPP LRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFA MPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARII GVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPL WGKVLKGKVIYTIKDGKMVYKD 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 DOR A 425 source : AC2 6) chain A residue 65 type sequence R description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 7) chain A residue 95 type sequence N description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 8) chain A residue 153 type sequence D description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 9) chain A residue 154 type sequence G description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 10) chain A residue 277 type sequence V description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 11) chain A residue 278 type sequence N description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 12) chain A residue 309 type sequence H description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 13) chain A residue 322 type sequence P description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 14) chain A residue 323 type sequence G description BINDING SITE FOR RESIDUE DOR A 425 source : AC2 15) chain A residue 101 type sequence D description BINDING SITE FOR RESIDUE EDO B 301 source : AC8 16) chain A residue 102 type sequence N description BINDING SITE FOR RESIDUE EDO B 301 source : AC8 17) chain A residue 103 type sequence T description BINDING SITE FOR RESIDUE EDO B 301 source : AC8 18) chain A residue 138 type sequence D description BINDING SITE FOR RESIDUE EDO B 301 source : AC8 19) chain A residue 101 type sequence D description BINDING SITE FOR RESIDUE EDO B 307 source : BC5 20) chain A residue 102 type sequence N description BINDING SITE FOR RESIDUE EDO B 307 source : BC5 21) chain A residue 222 type sequence Q description BINDING SITE FOR RESIDUE EDO B 310 source : BC8 22) chain A residue 240 type sequence E description BINDING SITE FOR RESIDUE EDO B 310 source : BC8 23) chain A residue 140 type sequence Y description BINDING SITE FOR RESIDUE EDO B 311 source : BC9 24) chain A residue 200 type sequence L description BINDING SITE FOR RESIDUE EDO B 312 source : CC1 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) chain A residue 59-67 type prosite sequence DIHVHLRDP description DIHYDROOROTASE_1 Dihydroorotase signature 1. DIHVHLRdP source prosite : PS00482 34) chain A residue 303-314 type prosite sequence ATDHAPHQTFEK description DIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHqtfeK source prosite : PS00483

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