1MOS
ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH 2-AMINO-2-DEOXYGLUCITOL 6-PHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004360 | molecular_function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity |
A | 0097367 | molecular_function | carbohydrate derivative binding |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
A | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 611 |
Chain | Residue |
A | HOH164 |
A | ALA393 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 612 |
Chain | Residue |
A | HIS465 |
A | HIS465 |
A | HIS466 |
A | HIS466 |
A | ASP513 |
A | ASP513 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 613 |
Chain | Residue |
A | GLN542 |
A | GLY540 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 614 |
Chain | Residue |
A | HOH22 |
A | HOH23 |
A | HOH26 |
A | HOH73 |
A | MES610 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE AGP A 609 |
Chain | Residue |
A | HOH13 |
A | HOH14 |
A | HOH61 |
A | HOH62 |
A | HOH82 |
A | HOH147 |
A | CYS300 |
A | GLY301 |
A | THR302 |
A | SER303 |
A | SER347 |
A | GLN348 |
A | SER349 |
A | THR352 |
A | VAL399 |
A | ALA400 |
A | SER401 |
A | LYS485 |
A | GLU488 |
A | HIS504 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MES A 610 |
Chain | Residue |
A | HOH29 |
A | HOH55 |
A | HOH59 |
A | ALA520 |
A | ASN522 |
A | GLU569 |
A | NA614 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: For Fru-6P isomerization activity |
Chain | Residue | Details |
A | SER604 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
A | LYS603 | |
A | LYS485 | |
A | GLU488 | |
A | GLU481 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
A | HIS504 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 82 |
Chain | Residue | Details |
A | GLY482 | electrostatic stabiliser, hydrogen bond acceptor |
A | LEU486 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ILE489 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLY505 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | SER604 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |