Structure of PDB 1a9x Chain E

Receptor sequence

>1a9xE (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: E
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K4202 D4338 G4507 K4634 D4769 P4901
• 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	E	E4299 N4301	E299 N301
BS02	MN	E	Q4285 E4299	Q285 E299
BS03	PO4	E	G4175 E4299 N4301 R4303 R4306	G175 E299 N301 R303 R306
BS04	MN	E	Q4829 E4841	Q814 E826
BS05	ADP	E	R4129 I4167 R4169 M4174 G4175 G4176 E4208 L4210 I4211 E4215 M4240 G4241 I4242 H4243 T4244 Q4285 E4299 T4376	R129 I167 R169 M174 G175 G176 E208 L210 I211 E215 M240 G241 I242 H243 T244 Q285 E299 T376
BS06	ADP	E	V4713 R4715 M4725 F4755 L4756 E4761 A4785 G4786 V4787 H4788 E4841	V713 R715 M718 F740 L741 E746 A770 G771 V772 H773 E826
BS07	ORN	E	E4783 D4791 E4892 L4895 Y5040 D5041 T5042	E768 D776 E877 L880 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)