Structure of PDB 1t36 Chain A

Receptor sequence

>1t36A (length=1058) Species: 562 (Escherichia coli)

MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSN
PATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCAL
ELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAH
TMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSP
TKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITV
APAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEM
NPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEP
SIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALR
GLEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVD
GVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADA
RLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEE
CEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVN
CNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKL
ARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEM
AVEKAKEIGYPLVVRPAMEIVYDEADLRRYFQTAVLLDHFLDDAVEVDVD
AICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQK
LAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVA
ARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTG
EVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLAAKLL
KQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIIN
TTSGRRAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISV
QEMHAQIK

3D structure

• PDB: 1t36 Long-range allosteric transitions in carbamoyl phosphate synthetase.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R129 R169 M174 G176 K202 E215 H243 N283 Q285 E299 N301 R303 S307 D338 G507 K634 R715 E761 D769 Q829 E841 N843 R848 P901
• Catalytic site (residue number reindexed from 1): R129 R169 M174 G176 K202 E215 H243 N283 Q285 E299 N301 R303 S307 D338 G507 K634 R715 E746 D754 Q814 E826 N828 R833 P886
• Enzyme Commision number: 6.3.4.16: carbamoyl-phosphate synthase (ammonia).
  6.3.5.5: carbamoyl-phosphate synthase (glutamine-hydrolyzing).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MN	A	E299 N301	E299 N301
BS02	MN	A	Q285 E299	Q285 E299
BS03	PO4	A	M174 G175 H243 E299 N301 R303 R306	M174 G175 H243 E299 N301 R303 R306
BS04	MN	A	Q829 E841	Q814 E826
BS05	ADP	A	R129 I167 R169 M174 G175 G176 E208 L210 I211 E215 M240 G241 I242 H243 Q285 I298 E299 T376	R129 I167 R169 M174 G175 G176 E208 L210 I211 E215 M240 G241 I242 H243 Q285 I298 E299 T376
BS06	ADP	A	R715 M725 F755 L756 E761 A785 G786 V787 H788 E841 P909	R715 M718 F740 L741 E746 A770 G771 V772 H773 E826 P894
BS07	ORN	A	E783 D791 E892 L907 D1041 T1042	E768 D776 E877 L892 D1026 T1027
BS08	U	A	K954 T974 G976 T977 K993 N1015 T1016 T1017 S1026 I1029	K939 T959 G961 T962 K978 N1000 T1001 T1002 S1011 I1014	MOAD: Kd=9uM

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004087 carbamoyl-phosphate synthase (ammonia) activity
• GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016597 amino acid binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0006526 L-arginine biosynthetic process
• GO:0006541 glutamine metabolic process
• GO:0008652 amino acid biosynthetic process
• GO:0019856 pyrimidine nucleobase biosynthetic process
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0005951 carbamoyl-phosphate synthase complex

External links

• PDB: RCSB:1t36, PDBe:1t36, PDBj:1t36
• PDBsum: 1t36
• PubMed: 15322282
• UniProt: P00968|CARB_ECOLI Carbamoyl phosphate synthase large chain (Gene Name=carB)