eF-site ID 3lxm-A PDB Code 3lxm Chain A click to enlarge Title 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia pestis CO92 Classification TRANSFERASE Compound Aspartate carbamoyltransferase Source Yersinia pestis (PYRB_YERPE) Sequence A:  ANPLYHKHIISINDLSRDELELVLRTAASLKKTPQPELLK HKVIASCFFEASTRTRLSFETSIHRLGASVVGFSDGETLA DTMSVISTYVDAIVMRHPQEGASRLAAQFSGNVPIVNAGD GANQHPTQTLLDLFTIQETQGRLDNINIAMVGDLKYGRTV HSLTQALAKFNGNHFFFIAPDALAMPAYILQMLEEKEIEY SLHESLEEVVPELDILYMTRYANVKAQFILRSSDLTGARD NLKVLHPLPRIDEITTDVDKTPYAYYFQQAGNGIFARQAL LALVLNAELA Description Functional site 1) chain A residue 52 type sequence A description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 2) chain A residue 53 type sequence S description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 3) chain A residue 54 type sequence T description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 4) chain A residue 55 type sequence R description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 5) chain A residue 56 type sequence T description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 6) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 7) chain A residue 135 type sequence H description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 8) chain A residue 230 type sequence R description BINDING SITE FOR RESIDUE PG4 A 312 source : AC1 9) chain A residue 49-56 type prosite sequence FFEASTRT description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FfEaSTRT source prosite : PS00097 10) chain A residue 55 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 269 type BINDING sequence P description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 56 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 106 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 135 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 138 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 168 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 230 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 268 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_00001 source Swiss-Prot : SWS_FT_FI1

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