Structure of PDB 1a9x Chain G

Receptor sequence

>1a9xG (length=1058) Species: 562 (Escherichia coli)

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

3D structure

• PDB: 1a9x Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.
• Chain: G
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R6129 R6169 K6202 E6215 H6243 N6283 Q6285 E6299 N6301 R6303 S6307 D6338 G6507 K6634 R6715 E6761 D6769 Q6829 E6841 N6843 R6848 P6901
• Catalytic site (residue number reindexed from 1): R129 R169 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	G	M6174 E6299 N6301	M174 E299 N301
BS02	MN	G	Q6285 E6299	Q285 E299
BS03	PO4	G	M6174 G6175 E6299 N6301 R6303 R6306	M174 G175 E299 N301 R303 R306
BS04	MN	G	Q6829 E6841	Q814 E826
BS05	ADP	G	R6129 I6167 R6169 M6174 G6175 G6176 L6210 E6215 M6240 G6241 I6242 H6243 T6244 Q6285 E6299 T6376	R129 I167 R169 M174 G175 G176 L210 E215 M240 G241 I242 H243 T244 Q285 E299 T376
BS06	ADP	G	R6715 M6725 F6755 L6756 E6761 A6785 G6786 H6788 E6841	R715 M718 F740 L741 E746 A770 G771 H773 E826
BS07	ORN	G	E6783 D6791 E6892 L6907 Y7040 D7041 T7042	E768 D776 E877 L892 Y1025 D1026 T1027

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:1a9x, PDBe:1a9x, PDBj:1a9x
• PDBsum: 1a9x
• PubMed: 9636022
• UniProt: P00968|CARB_ECOLI Carbamoyl phosphate synthase large chain (Gene Name=carB)