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3L8E

Crystal Structure of apo form of 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
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008270molecular_functionzinc ion binding
B0009103biological_processlipopolysaccharide biosynthetic process
B0009244biological_processlipopolysaccharide core region biosynthetic process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0034200molecular_functionD-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity
B0046872molecular_functionmetal ion binding
B0097171biological_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 801
ChainResidue
ACYS92
AHIS94
ACYS107
ACYS109
AARG110

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 901
ChainResidue
AASN54
ALYS111
ALYS137
AHOH202
AASP11
AARG12
AASP13
ATHR53

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 802
ChainResidue
BCYS92
BHIS94
BCYS107
BCYS109
BARG110

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 902
ChainResidue
BASP11
BARG12
BASP13
BTHR53
BASN54
BLYS111
BLYS137
BHOH193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
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 Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20050699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
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 Residues2
DetailsSite: {"description":"Contributes to substrate recognition","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Stabilizes the phosphoryl group","evidences":[{"source":"PubMed","id":"20050614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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