1Z84
X-ray structure of galt-like protein from arabidopsis thaliana at5g18200
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 603 |
Chain | Residue |
A | CYS63 |
A | CYS66 |
A | HIS133 |
A | HIS184 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 604 |
Chain | Residue |
A | CYS216 |
A | CYS219 |
A | HIS255 |
A | HIS310 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 605 |
Chain | Residue |
B | PHE65 |
B | CYS66 |
B | HIS133 |
B | HIS184 |
B | CYS63 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 606 |
Chain | Residue |
B | CYS216 |
B | CYS219 |
B | HIS255 |
B | HIS310 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AMP A 601 |
Chain | Residue |
A | PHE65 |
A | GLU72 |
A | CYS73 |
A | ALA74 |
A | ILE92 |
A | GLU93 |
A | ASN94 |
A | LEU95 |
A | TYR96 |
A | ASN173 |
A | ALA180 |
A | SER181 |
A | MET182 |
A | HIS186 |
A | GLN188 |
A | HOH611 |
A | HOH764 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AMP B 602 |
Chain | Residue |
B | PHE65 |
B | GLU72 |
B | CYS73 |
B | ALA74 |
B | ILE92 |
B | GLU93 |
B | ASN94 |
B | LEU95 |
B | TYR96 |
B | VAL126 |
B | ASN173 |
B | ALA180 |
B | SER181 |
B | MET182 |
B | HIS186 |
B | GLN188 |
B | HOH630 |
B | HOH679 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 607 |
Chain | Residue |
A | ALA242 |
A | TYR244 |
A | PRO245 |
A | PHE246 |
A | GLU247 |
A | ASN334 |
A | VAL336 |
A | PRO338 |
A | VAL341 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 608 |
Chain | Residue |
A | THR31 |
A | THR198 |
A | HIS295 |
A | GLN314 |
A | HOH616 |
A | HOH635 |
A | HOH668 |
A | HOH771 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 609 |
Chain | Residue |
A | TYR244 |
A | VAL316 |
A | GLN318 |
A | SER320 |
A | HOH632 |
A | HOH662 |
A | HOH742 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 610 |
Chain | Residue |
B | ALA238 |
B | ALA242 |
B | TYR244 |
B | PRO245 |
B | PHE246 |
B | GLU247 |
B | ASN334 |
B | VAL336 |
B | PRO338 |
B | VAL341 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 611 |
Chain | Residue |
B | THR31 |
B | THR198 |
B | HIS295 |
B | GLN314 |
B | HOH636 |
B | HOH678 |
B | HOH694 |
B | HOH820 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 612 |
Chain | Residue |
B | HOH687 |
B | HOH706 |
B | TYR244 |
B | VAL316 |
B | GLN318 |
B | SER320 |
B | HOH646 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:16519510, ECO:0000269|PubMed:17850744 |
Chain | Residue | Details |
A | HIS186 | |
B | HIS186 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ARG41 | |
B | GLU72 | |
B | ASN94 | |
B | ASN173 | |
B | GLY179 | |
B | GLN188 | |
B | GLY321 | |
B | PHE325 | |
A | GLU72 | |
A | ASN94 | |
A | ASN173 | |
A | GLY179 | |
A | GLN188 | |
A | GLY321 | |
A | PHE325 | |
B | ARG41 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16519510, ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | CYS63 | |
B | CYS66 | |
B | HIS133 | |
B | HIS184 | |
B | CYS216 | |
B | CYS219 | |
B | HIS255 | |
B | HIS310 | |
A | CYS66 | |
A | HIS133 | |
A | HIS184 | |
A | CYS216 | |
A | CYS219 | |
A | HIS255 | |
A | HIS310 | |
B | CYS63 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1hxq |
Chain | Residue | Details |
A | HIS186 | |
A | ALA180 | |
A | HIS184 | |
A | GLN188 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1hxq |
Chain | Residue | Details |
B | HIS186 | |
B | ALA180 | |
B | HIS184 | |
B | GLN188 |