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2HSE

Structure of D236A E. coli Aspartate Transcarbamoylase in the presence of phosphonoacetamide and l-Aspartate at 2.60 A resolution

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, C
(A, C)
Aspartate carbamoyltransferase catalytic chainpolymer31034293.12UniProt (P0A786)
Pfam (PF02729)
Pfam (PF00185)
Escherichia coliAspartate transcarbamylase, ATCase
2B, D
(B, D)
Aspartate carbamoyltransferase regulatory chainpolymer15317143.62UniProt (P0A7F3)
Pfam (PF01948)
Pfam (PF02748)
Escherichia coli
3E
(A)
PHOSPHATE IONnon-polymer95.01Chemie (PO4)
4F, J
(A, C)
PHOSPHONOACETAMIDEnon-polymer139.02Chemie (PCT)
5G, H, K
(A, C)
ASPARTIC ACIDnon-polymer133.13Chemie (ASP)
6I, L
(B, D)
ZINC IONnon-polymer65.42Chemie (ZN)
7M, N, O, P
(A, B, C, D)
waterwater18.0349Chemie (HOH)
Sequence modifications
A, C: 1 - 310 (UniProt: P0A786)
PDBExternal DatabaseDetails
Ala 236Asp 236engineered mutation
B, D: 2 - 153 (UniProt: P0A7F3)
PDBExternal DatabaseDetails
Met 1-initiating methionine
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains4
Total formula weight102873.4
Non-Polymers*Number of molecules8
Total formula weight903.2
All*Total formula weight103776.6
*Water molecules are not included.

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PDB entries from 2025-12-17

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