Structure of PDB 1c3o Chain C

Receptor sequence

>1c3oC (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: 1c3o The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway.
• Chain: C
• 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	C	E299 N301	E299 N301
BS02	MN	C	Q285 E299	Q285 E299
BS03	MN	C	Q829 E841	Q814 E826
BS04	PO4	C	M174 G175 H243 E299 N301 R303 R306	M174 G175 H243 E299 N301 R303 R306
BS05	ORN	C	D791 E892 V893 L907 Y1040 D1041 T1042	D776 E877 V878 L892 Y1025 D1026 T1027
BS06	GLN	C	R528 A537 T538 E552 N554	R528 A537 T538 E552 N554
BS07	ADP	C	R129 I167 R169 M174 G176 E208 L210 I211 E215 M240 H243 Q285 E299 T376	R129 I167 R169 M174 G176 E208 L210 I211 E215 M240 H243 Q285 E299 T376
BS08	ADP	C	R715 M725 F755 L756 E761 A785 G786 V787 H788 S789 E841	R715 M718 F740 L741 E746 A770 G771 V772 H773 S774 E826

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:1c3o, PDBe:1c3o, PDBj:1c3o
• PDBsum: 1c3o
• PubMed: 10587438
• UniProt: P00968|CARB_ECOLI Carbamoyl phosphate synthase large chain (Gene Name=carB)