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3ESQ

Crystal Structure of Calcium-bound D,D-heptose 1.7-bisphosphate phosphatase from E. Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008270molecular_functionzinc ion binding
A0009103biological_processlipopolysaccharide biosynthetic process
A0009244biological_processlipopolysaccharide core region biosynthetic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0034200molecular_functionD-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity
A0046872molecular_functionmetal ion binding
A0097171biological_processADP-L-glycero-beta-D-manno-heptose biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 212
ChainResidue
ACYS112
AHIS114
ACYS127
ACYS129
AARG130

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 213
ChainResidue
AHOH385
AHOH386
AASP31
AASP33
AASP156
AHOH384

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Stabilizes the phosphoryl group","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Contributes to substrate recognition","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Stabilizes the phosphoryl group","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
AALA100
ALYS131

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ALYS131
ATHR73

239803

PDB entries from 2025-08-06

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