Structure of PDB 1ml4 Chain A Binding Site BS01

Receptor Information
>1ml4 Chain A (length=307) Species: 29292 (Pyrococcus abyssi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DWKGRDVISIRDFSKEDIETVLATAERLERELKEKGQLEYAKGKILATLF
FEPSTRTRLSFESAMHRLGGAVIGFAEASTSSVKKGESLRDTIKTVEQYC
DVIVIRHPKEGAARLAAEVAEVPVINAGDGSNQHPTQTLLDLYTIKKEFG
RIDGLKIGLLGDLKYGRTVHSLAEALTFYDVELYLISPELLRMPRHIVEE
LREKGMKVVETTTLEDVIGKLDVLYVTRIQKERFPDEQEYLKVKGSYQVN
LKVLEKAKDELRIMHPLPRVDEIHPEVDNTKHAIYFRQVFNGVPVRMALL
ALVLGVI
Ligand information
Ligand IDPAL
InChIInChI=1S/C6H10NO8P/c8-4(2-16(13,14)15)7-3(6(11)12)1-5(9)10/h3H,1-2H2,(H,7,8)(H,9,10)(H,11,12)(H2,13,14,15)/t3-/m0/s1
InChIKeyZZKNRXZVGOYGJT-VKHMYHEASA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)C[CH](NC(=O)C[P](O)(O)=O)C(O)=O
CACTVS 3.341OC(=O)C[C@H](NC(=O)C[P](O)(O)=O)C(O)=O
ACDLabs 10.04O=C(NC(C(=O)O)CC(=O)O)CP(=O)(O)O
OpenEye OEToolkits 1.5.0C(C(C(=O)O)NC(=O)CP(=O)(O)O)C(=O)O
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)NC(=O)CP(=O)(O)O)C(=O)O
FormulaC6 H10 N O8 P
NameN-(PHOSPHONACETYL)-L-ASPARTIC ACID
ChEMBLCHEMBL504802
DrugBankDB03459
ZINCZINC000001563934
PDB chain1ml4 Chain A Residue 385 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ml4 Aspartate Transcarbamylase from the Hyperthermophilic Archaeon Pyrococcus abyssi: Thermostability and 1.8A Resolution Crystal Structure of the Catalytic Subunit Complexed With the Bisubstrate Analogue N-Phosphonacetyl-L-aspartate.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		S55 T56 R57 T58 R107 H135 R168 T169 R229 L268
Binding residue
(residue number reindexed from 1)		S54 T55 R56 T57 R106 H134 R167 T168 R228 L267
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R57 T58 K86 R107 H135 Q138 T228 P267 G293
Catalytic site (residue number reindexed from 1) R56 T57 K85 R106 H134 Q137 T227 P266 G292
Enzyme Commision number 2.1.3.2: aspartate carbamoyltransferase.
Gene Ontology
Molecular Function
GO:0004070 aspartate carbamoyltransferase activity
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006520 amino acid metabolic process
GO:0044205 'de novo' UMP biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ml4, PDBe:1ml4, PDBj:1ml4
PDBsum1ml4
PubMed12547202
UniProtP77918|PYRB_PYRAB Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)

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