eF-site ID 3at1-C PDB Code 3at1 Chain C click to enlarge Title CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE) Compound ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN Source Escherichia coli (strain K12) (PYRI_ECOLI) Sequence C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT PHAWYFQQAGNGIFARQALLALVLNRDLVL Description Functional site 1) chain C residue 54 type sequence R description PCT binding site source : PAC 2) chain C residue 55 type sequence T description PCT binding site source : PAC 3) chain C residue 105 type sequence R description PCT binding site source : PAC 4) chain C residue 134 type sequence H description PCT binding site source : PAC 5) chain C residue 137 type sequence Q description PCT binding site source : PAC 6) chain C residue 266 type sequence P description PCT binding site source : PAC 7) chain C residue 267 type sequence L description PCT binding site source : PAC 8) chain C residue 52 type sequence S description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 9) chain C residue 54 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 10) chain C residue 55 type sequence T description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 11) chain C residue 105 type sequence R description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 12) chain C residue 137 type sequence Q description BINDING SITE FOR RESIDUE PCT C 311 source : AC4 13) chain C residue 55 type catalytic sequence T description 405 source MCSA : MCSA2 14) chain C residue 56 type catalytic sequence R description 405 source MCSA : MCSA2 15) chain C residue 85 type catalytic sequence G description 405 source MCSA : MCSA2 16) chain C residue 106 type catalytic sequence H description 405 source MCSA : MCSA2 17) chain C residue 135 type catalytic sequence P description 405 source MCSA : MCSA2 18) chain C residue 106 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 19) chain C residue 135 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 20) chain C residue 138 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 21) chain C residue 268 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 22) chain C residue 269 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 23) chain C residue 56 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 24) chain C residue 85 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 168 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787 source Swiss-Prot : SWS_FT_FI2 26) chain C 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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