1C7Z
REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 401 |
Chain | Residue |
A | ARG8 |
A | HIS9 |
A | ASN15 |
A | ARG58 |
A | GLU78 |
A | HIS143 |
A | GLN144 |
A | G3H501 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 402 |
Chain | Residue |
B | HIS9 |
B | ASN15 |
B | ARG58 |
B | GLU78 |
B | HIS143 |
B | GLN144 |
B | G3H502 |
B | HOH505 |
B | ARG8 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE G3H A 501 |
Chain | Residue |
A | TYR89 |
A | ARG103 |
A | LYS107 |
A | TYR118 |
A | GLN144 |
A | ALA145 |
A | ARG148 |
A | PO4401 |
A | HOH582 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE G3H B 502 |
Chain | Residue |
B | GLU78 |
B | TYR89 |
B | ARG103 |
B | LYS107 |
B | TYR118 |
B | GLN144 |
B | ALA145 |
B | ARG148 |
B | PO4402 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN |
Chain | Residue | Details |
A | LEU6-ASN15 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16875","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9253407","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 14 |
Details | Binding 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."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00950","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | ARG58 | |
A | HIS143 | |
A | GLU78 | |
A | HIS9 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | ARG58 | |
B | HIS143 | |
B | GLU78 | |
B | HIS9 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | ARG58 | |
A | ASN15 | |
A | ARG8 | |
A | HIS143 | |
A | GLU78 | |
A | HIS9 |
site_id | CSA4 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | ARG58 | |
B | ASN15 | |
B | ARG8 | |
B | HIS143 | |
B | GLU78 | |
B | HIS9 |