eF-site ID 1a9x-D PDB Code 1a9x Chain D click to enlarge Title CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS Classification AMIDOTRANSFERASE Compound CARBAMOYL PHOSPHATE SYNTHETASE (LARGE CHAIN) Source Escherichia coli (strain K12) (CARA_ECOLI) Sequence D:  IKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQE ILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLV IRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRL LREKGAQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKE VTTAEAYSWTQGSWTLTGGLPQAKKEDELPFHVVAYDFGA KRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNG PGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGA KTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATL PANLRVTHKSLFDGTLQGIHRTDKPAFSFQGNPEASPGPH DAAPLFDHFIELIEQYRKT Description Functional site 1) chain D residue 3547 type sequence S description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 2) chain D residue 3741 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 3) chain D residue 3743 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 4) chain D residue 3773 type sequence Q description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 5) chain D residue 3813 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 6) chain D residue 3814 type sequence F description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY2 7) chain D residue 3515 type sequence F description BINDING SITE FOR RESIDUE CL D 3933 source : DC6 8) chain D residue 3614 type sequence D description BINDING SITE FOR RESIDUE CL D 3933 source : DC6 9) chain D residue 3516 type sequence H description BINDING SITE FOR RESIDUE K D 3941 source : EC2 10) chain D residue 3612 type sequence D description BINDING SITE FOR RESIDUE K D 3941 source : EC2 11) chain D residue 3769 type catalytic sequence X description 435 source MCSA : MCSA2 12) chain D residue 3853 type catalytic sequence N description 435 source MCSA : MCSA2 13) chain D residue 3855 type catalytic sequence E description 435 source MCSA : MCSA2 14) chain D residue 3769 type ACT_SITE sequence X description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 3853 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 3855 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 3741 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 18) chain D residue 3743 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 19) chain D residue 3770 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 20) chain D residue 3773 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 21) chain D residue 3811 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 22) chain D residue 3813 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 23) chain D residue 3814 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3 24) chain D residue 3547 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01209, ECO:0000269|PubMed:10587438, ECO:0007744|PDB:1C3O source Swiss-Prot : SWS_FT_FI3

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