Structure of PDB 1ml4 Chain A

Receptor sequence

>1ml4A (length=307) Species: 29292 (Pyrococcus abyssi)

DWKGRDVISIRDFSKEDIETVLATAERLERELKEKGQLEYAKGKILATLF
FEPSTRTRLSFESAMHRLGGAVIGFAEASTSSVKKGESLRDTIKTVEQYC
DVIVIRHPKEGAARLAAEVAEVPVINAGDGSNQHPTQTLLDLYTIKKEFG
RIDGLKIGLLGDLKYGRTVHSLAEALTFYDVELYLISPELLRMPRHIVEE
LREKGMKVVETTTLEDVIGKLDVLYVTRIQKERFPDEQEYLKVKGSYQVN
LKVLEKAKDELRIMHPLPRVDEIHPEVDNTKHAIYFRQVFNGVPVRMALL
ALVLGVI

3D structure

• PDB: 1ml4 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.
• Chain: A
• Resolution: 1.8 Å

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.

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	PAL	A	S55 T56 R57 T58 R107 H135 R168 T169 R229 L268	S54 T55 R56 T57 R106 H134 R167 T168 R228 L267

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

External links

• PDB: RCSB:1ml4, PDBe:1ml4, PDBj:1ml4
• PDBsum: 1ml4
• PubMed: 12547202
• UniProt: P77918|PYRB_PYRAB Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)