Structure of PDB 1a9x Chain C

Receptor sequence

>1a9xC (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: C
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K2202 D2338 G2507 K2634 D2769 P2901
• Catalytic site (residue number reindexed from 1): K202 D338 G507 K634 D754 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	C	E2299 N2301	E299 N301
BS02	MN	C	Q2285 E2299	Q285 E299
BS03	PO4	C	G2175 H2243 E2299 N2301 R2303 R2306	G175 H243 E299 N301 R303 R306
BS04	MN	C	Q2829 E2841	Q814 E826
BS05	ADP	C	R2129 I2167 R2169 M2174 G2176 L2210 I2211 E2215 M2240 G2241 I2242 H2243 T2244 Q2285 I2298 E2299 T2376	R129 I167 R169 M174 G176 L210 I211 E215 M240 G241 I242 H243 T244 Q285 I298 E299 T376
BS06	ADP	C	R2715 M2725 F2755 L2756 E2761 A2785 G2786 V2787 H2788 S2789 E2841	R715 M718 F740 L741 E746 A770 G771 V772 H773 S774 E826
BS07	ORN	C	E2783 D2791 E2892 V2893 L2907 Y3040 D3041 T3042	E768 D776 E877 V878 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)