6DVV
2.25 Angstrom Resolution Crystal Structure of 6-phospho-alpha-glucosidase from Klebsiella pneumoniae in Complex with NAD and Mn2+.
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 | 21 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | GLY12 |
| A | HIS84 |
| A | ILE85 |
| A | ARG86 |
| A | VAL87 |
| A | TYR90 |
| A | GLU109 |
| A | TYR118 |
| A | TYR145 |
| A | SER146 |
| A | ASN147 |
| A | SER13 |
| A | HOH604 |
| A | HOH643 |
| A | THR14 |
| A | PHE15 |
| A | ILE19 |
| A | ASP39 |
| A | ASN40 |
| A | ASP41 |
| A | ARG44 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 502 |
| Chain | Residue |
| A | ASN147 |
| A | CYS169 |
| A | HIS200 |
| A | HOH602 |
| A | HOH669 |
| A | HOH704 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ARG194 |
| A | THR205 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG157 |
| A | ARG158 |
| A | HOH610 |
| A | HOH636 |
| A | HOH655 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | TYR90 |
| A | ARG93 |
| A | TRP241 |
| A | ARG283 |
| A | ARG291 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 506 |
| Chain | Residue |
| A | PRO376 |
| A | HIS377 |
| A | HOH603 |
| A | HOH610 |
| A | HOH644 |
| A | HOH747 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 507 |
| Chain | Residue |
| A | GLN108 |
| A | LYS265 |
| A | TYR266 |
| A | ARG283 |
| A | HOH665 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | ASN147 |
| B | CYS169 |
| B | HIS200 |
| B | HOH622 |
| B | HOH722 |
| B | HOH752 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PHE350 |
| B | ASP351 |
| B | LYS380 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | SO4506 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | ARG93 |
| B | ARG283 |
| B | ARG291 |
| B | HOH686 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| B | ARG194 |
| B | THR205 |
| B | SER206 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 506 |
| Chain | Residue |
| B | PRO376 |
| B | HIS377 |
| B | LYS404 |
| B | CL503 |
| B | HOH641 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 507 |
| Chain | Residue |
| B | SER13 |
| B | THR14 |
| B | PHE15 |
| B | ARG44 |
| B | ARG86 |
| B | TYR90 |
| B | HOH618 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 508 |
| Chain | Residue |
| B | GLN181 |
| B | LYS186 |
| B | HOH673 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 509 |
| Chain | Residue |
| B | GLN108 |
| B | LYS265 |
| B | TYR266 |
| B | HOH605 |
| B | HOH662 |
| B | HOH714 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 510 |
| Chain | Residue |
| B | ARG157 |
| B | ARG158 |
| B | HOH613 |
| B | HOH659 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 511 |
| Chain | Residue |
| B | ARG283 |
| B | GLU286 |
| B | HIS290 |
| B | ARG291 |
| B | HOH732 |
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 |
