6DUX
2.25 Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Klebsiella pneumoniae in Complex with NAD.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005985 | biological_process | sucrose metabolic process |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050081 | molecular_function | maltose-6'-phosphate glucosidase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005985 | biological_process | sucrose metabolic process |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050081 | molecular_function | maltose-6'-phosphate glucosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | GLY12 |
| A | ILE85 |
| A | ARG86 |
| A | TYR90 |
| A | GLU109 |
| A | TYR118 |
| A | TYR145 |
| A | SER146 |
| A | ASN147 |
| A | HOH602 |
| A | HOH618 |
| A | SER13 |
| A | HOH625 |
| A | HOH633 |
| A | HOH637 |
| A | HOH686 |
| A | HOH716 |
| A | HOH741 |
| A | THR14 |
| A | PHE15 |
| A | ASP39 |
| A | ASN40 |
| A | ASP41 |
| A | ARG44 |
| A | HIS84 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue LMR A 502 |
| Chain | Residue |
| A | GLY104 |
| A | PRO270 |
| A | VAL274 |
| A | LYS413 |
| A | VAL415 |
| A | PRO416 |
| A | HOH604 |
| A | HOH752 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | THR14 |
| A | PRO17 |
| A | GLY18 |
| A | ARG291 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PRO376 |
| A | HIS377 |
| A | ASP395 |
| A | GLN399 |
| A | LYS404 |
| A | HOH603 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | HOH661 |
| B | GLU368 |
| B | HOH752 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | GLY12 |
| B | SER13 |
| B | THR14 |
| B | PHE15 |
| B | ILE19 |
| B | ASP39 |
| B | ASN40 |
| B | ASP41 |
| B | ARG44 |
| B | HIS84 |
| B | ILE85 |
| B | ARG86 |
| B | VAL87 |
| B | TYR90 |
| B | GLU109 |
| B | TYR118 |
| B | TYR145 |
| B | SER146 |
| B | ASN147 |
| B | GLU292 |
| B | HOH602 |
| B | HOH620 |
| B | HOH624 |
| B | HOH720 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue BCT B 502 |
| Chain | Residue |
| B | VAL183 |
| B | ASP209 |
| B | ASP209 |
| B | ASP211 |
| B | ASN213 |
| B | LYS218 |
| B | HOH667 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLY104 |
| B | LYS413 |
| B | THR414 |
| B | VAL415 |
| B | PRO416 |
| B | PRO416 |
| B | HOH676 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | TRP397 |
| B | ARG400 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | HOH752 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | HIS290 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 507 |
| Chain | Residue |
| B | ARG157 |
| B | HOH697 |
Functional Information from PROSITE/UniProt
| site_id | PS01324 |
| Number of Residues | 32 |
| Details | GLYCOSYL_HYDROL_F4 Glycosyl hydrolases family 4 signature. PnAwMLNysNPaaivAeatrrlrpna.KiLNiC |
| Chain | Residue | Details |
| A | PRO138-CYS169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Increases basicity of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
