eF-site ID 1d09-C PDB Code 1d09 Chain C click to enlarge Title ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA) Classification TRANSFERASE Compound ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN Source Escherichia coli (strain K12) (PYRI_ECOLI) Sequence C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTQGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL Description Functional site 1) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 2) chain C residue 53 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 3) chain C residue 54 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 4) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 5) chain C residue 80 type sequence S description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 6) chain C residue 84 type sequence K description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 7) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 8) chain C residue 134 type sequence H description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 9) chain C residue 167 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 10) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 11) chain C residue 229 type sequence R description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 12) chain C residue 267 type sequence L description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 13) chain C residue 268 type sequence P description BINDING SITE FOR RESIDUE PAL C 1312 source : AC4 14) chain C residue 54 type catalytic sequence R description 405 source MCSA : MCSA2 15) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 16) chain C residue 84 type catalytic sequence K description 405 source MCSA : MCSA2 17) chain C residue 105 type catalytic sequence R description 405 source MCSA : MCSA2 18) chain C residue 134 type catalytic sequence H description 405 source MCSA : MCSA2 19) chain C residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 20) chain C residue 134 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 21) chain C residue 137 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 22) chain C residue 267 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI1 23) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 24) chain C residue 55 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 25) chain C residue 84 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 167 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 229 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2

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