Structure of PDB 1a9x Chain E Binding Site BS01

Receptor Information
>1a9x Chain E (length=1058) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVINVNSN
PATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCAL
ELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAH
TMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSP
TKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITV
APAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEM
NPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEP
SIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALR
GLEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVD
GVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADA
RLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEE
CEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVN
CNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKL
ARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEM
AVEKAKEIGYPLVVRAAMEIVYDEADLRRYFQTAVLLDHFLDDAVEVDVD
AICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQK
LAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVA
ARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTG
EVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLAAKLL
KQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIIN
TTSGRRAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISV
QEMHAQIK
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1a9x Chain E Residue 5901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1a9x Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		E4299 N4301
Binding residue
(residue number reindexed from 1)		E299 N301
Annotation score1
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).
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1a9x, PDBe:1a9x, PDBj:1a9x
PDBsum1a9x
PubMed9636022
UniProtP00968|CARB_ECOLI Carbamoyl phosphate synthase large chain (Gene Name=carB)

[Back to BioLiP]