2H39
Crystal Structure of an ADP-Glucose Phosphorylase from Arabidopsis thaliana with bound ADP-Glucose
Replaces: 2GDKFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0017103 | molecular_function | UTP:galactose-1-phosphate uridylyltransferase activity |
| A | 0043531 | molecular_function | ADP binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047345 | molecular_function | ribose-5-phosphate adenylyltransferase activity |
| A | 0080040 | biological_process | positive regulation of cellular response to phosphate starvation |
| B | 0005634 | cellular_component | nucleus |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0008108 | molecular_function | UDP-glucose:hexose-1-phosphate uridylyltransferase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0017103 | molecular_function | UTP:galactose-1-phosphate uridylyltransferase activity |
| B | 0043531 | molecular_function | ADP binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047345 | molecular_function | ribose-5-phosphate adenylyltransferase activity |
| B | 0080040 | biological_process | positive regulation of cellular response to phosphate starvation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 352 |
| Chain | Residue |
| A | CYS63 |
| A | CYS66 |
| A | HIS133 |
| A | HIS184 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 353 |
| Chain | Residue |
| A | CYS216 |
| A | CYS219 |
| A | HIS255 |
| A | HIS310 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 352 |
| Chain | Residue |
| B | CYS66 |
| B | HIS133 |
| B | HIS184 |
| B | CYS63 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 353 |
| Chain | Residue |
| B | CYS216 |
| B | CYS219 |
| B | HIS255 |
| B | HIS310 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 401 |
| Chain | Residue |
| B | PHE259 |
| B | HIS260 |
| B | THR296 |
| B | HOH611 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 402 |
| Chain | Residue |
| A | PHE259 |
| A | HIS260 |
| A | THR296 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ADQ A 506 |
| Chain | Residue |
| A | PHE65 |
| A | GLU72 |
| A | CYS73 |
| A | ALA74 |
| A | ILE92 |
| A | GLU93 |
| A | ASN94 |
| A | LEU95 |
| A | TYR96 |
| A | PHE171 |
| A | ASN173 |
| A | GLY179 |
| A | ALA180 |
| A | SER181 |
| A | MET182 |
| A | GLN188 |
| A | HOH559 |
| A | HOH614 |
| A | HOH615 |
| A | HOH687 |
| A | HOH690 |
| B | ARG41 |
| B | ARG44 |
| B | GLY321 |
| B | GLY323 |
| B | GLY324 |
| B | PHE325 |
| B | GLU326 |
| B | ILE333 |
| B | HOH544 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADQ B 507 |
| Chain | Residue |
| A | ARG41 |
| A | ARG44 |
| A | GLY321 |
| A | GLY323 |
| A | GLY324 |
| A | PHE325 |
| A | GLU326 |
| B | PHE65 |
| B | GLU72 |
| B | CYS73 |
| B | ALA74 |
| B | ILE92 |
| B | GLU93 |
| B | ASN94 |
| B | LEU95 |
| B | TYR96 |
| B | ASN173 |
| B | GLY179 |
| B | ALA180 |
| B | SER181 |
| B | MET182 |
| B | GLN188 |
| B | HOH537 |
| B | HOH546 |
| B | HOH629 |
| B | HOH672 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-AMP-histidine intermediate","evidences":[{"source":"PubMed","id":"16519510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of an ADP-glucose phosphorylase from Arabidopsis thaliana with bound ADP-glucose.","authors":["McCoy J.G.","Wesenberg G.E.","Phillips G.N. Jr.","Bitto E.","Bingman C.A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16519510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of an ADP-glucose phosphorylase from Arabidopsis thaliana with bound ADP-glucose.","authors":["McCoy J.G.","Wesenberg G.E.","Phillips G.N. Jr.","Bitto E.","Bingman C.A."]}}]} |
| Chain | Residue | Details |
