eF-site ID 1a9x-B PDB Code 1a9x Chain B 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 B:  IKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQE ILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLV IRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRL LREKGAQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKE VTTAEAYSWTQGSWTLTGGLPQAKKEDELPFHVVAYDFGA KRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNG PGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGA KTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATL PANLRVTHKSLFDGTLQGIHRTDKPAFSFQGNPEASPGPH DAAPLFDHFIELIEQYRKT Description Functional site 1) chain B residue 1547 type sequence S description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 2) chain B residue 1741 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 3) chain B residue 1743 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 4) chain B residue 1773 type sequence Q description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 5) chain B residue 1813 type sequence G description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 6) chain B residue 1814 type sequence F description BINDING SITE FOR GLUTAMYL THIOESTERMEDIATE IN SMALL SUBUNIT. source : CY1 7) chain B residue 1614 type sequence D description BINDING SITE FOR RESIDUE CL B 1933 source : IC7 8) chain B residue 1516 type sequence H description BINDING SITE FOR RESIDUE K B 1941 source : JC3 9) chain B residue 1612 type sequence D description BINDING SITE FOR RESIDUE K B 1941 source : JC3 10) chain B residue 1769 type catalytic sequence X description 435 source MCSA : MCSA1 11) chain B residue 1853 type catalytic sequence N description 435 source MCSA : MCSA1 12) chain B residue 1855 type catalytic sequence E description 435 source MCSA : MCSA1 13) chain B residue 1769 type ACT_SITE sequence X description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 1853 type ACT_SITE sequence N description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 1855 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01209 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 1547 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 17) chain B residue 1741 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 B residue 1743 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 B residue 1770 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 B residue 1773 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 B residue 1811 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 B residue 1813 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 B residue 1814 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

Display surface Download Links