eF-site ID 2air-G PDB Code 2air Chain G click to enlarge Title T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme Classification TRANSFERASE Compound Aspartate carbamoyltransferase catalytic chain Source (PYRI_ECOLI) Sequence G:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL Description Functional site 1) chain G residue 54 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 2) chain G residue 55 type sequence T description BINDING SITE FOR RESIDUE CP G 803 source : AC4 3) chain G residue 105 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 4) chain G residue 134 type sequence H description BINDING SITE FOR RESIDUE CP G 803 source : AC4 5) chain G residue 229 type sequence R description BINDING SITE FOR RESIDUE CP G 803 source : AC4 6) chain G residue 51 type sequence A description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 7) chain G residue 52 type sequence S description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 8) chain G residue 54 type sequence R description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 9) chain G residue 55 type sequence T description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 10) chain G residue 80 type sequence S description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 11) chain G residue 105 type sequence R description BINDING SITE FOR RESIDUE AL0 G 804 source : AC5 12) chain G residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 13) chain G residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 14) chain G residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 15) chain G residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 16) chain G residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 17) chain G residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 18) chain G residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 19) chain G residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 20) chain G residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 21) chain G residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 22) chain G residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 23) chain G residue 85 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 24) chain G residue 168 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 25) chain G residue 230 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2

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