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1C7Z

REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0006003biological_processfructose 2,6-bisphosphate metabolic process
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0006003biological_processfructose 2,6-bisphosphate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
AARG8
AHIS9
AASN15
AARG58
AGLU78
AHIS143
AGLN144
AG3H501

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 402
ChainResidue
BHIS9
BASN15
BARG58
BGLU78
BHIS143
BGLN144
BG3H502
BHOH505
BARG8

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE G3H A 501
ChainResidue
ATYR89
AARG103
ALYS107
ATYR118
AGLN144
AALA145
AARG148
APO4401
AHOH582

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE G3H B 502
ChainResidue
BGLU78
BTYR89
BARG103
BLYS107
BTYR118
BGLN144
BALA145
BARG148
BPO4402

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN
ChainResidueDetails
ALEU6-ASN15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q16875","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2000","submissionDatabase":"PDB data bank","title":"Reaction mechanism of fructose-2,6-bisphosphatase suggested by the crystal structures of a pseudo-Michaelis complex and metabolite complexes.","authors":["Lee Y.-H.","Olson T.W.","McClard R.W.","Witte J.F.","McFarlan S.C.","Banaszak L.J.","Levitt D.G.","Lange A.J."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00950","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG58
AHIS143
AGLU78
AHIS9

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG58
BHIS143
BGLU78
BHIS9

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG58
AASN15
AARG8
AHIS143
AGLU78
AHIS9

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG58
BASN15
BARG8
BHIS143
BGLU78
BHIS9

239803

PDB entries from 2025-08-06

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