3PN8
The crystal structure of 6-phospho-beta-glucosidase from Streptococcus mutans UA159
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008706 | molecular_function | 6-phospho-beta-glucosidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0103047 | molecular_function | methyl beta-D-glucoside 6-phosphate glucohydrolase activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008706 | molecular_function | 6-phospho-beta-glucosidase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0103047 | molecular_function | methyl beta-D-glucoside 6-phosphate glucohydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 478 |
Chain | Residue |
A | TRP349 |
A | SER430 |
A | ALA431 |
A | GLY432 |
A | LYS438 |
A | TYR440 |
A | HOH620 |
A | HOH654 |
A | HOH689 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 479 |
Chain | Residue |
A | ARG437 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 480 |
Chain | Residue |
A | PHE292 |
A | THR293 |
A | GLU294 |
A | LYS297 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 481 |
Chain | Residue |
A | ASN249 |
A | LYS251 |
A | HOH617 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 482 |
Chain | Residue |
A | LYS251 |
A | TYR328 |
A | HOH748 |
A | HOH772 |
B | HOH676 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 483 |
Chain | Residue |
A | ARG147 |
A | ASP151 |
A | ARG220 |
A | ARG295 |
A | HOH758 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 484 |
Chain | Residue |
A | ARG162 |
A | LYS165 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 485 |
Chain | Residue |
A | ASN7 |
A | LEU417 |
A | MSE418 |
A | HOH537 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 486 |
Chain | Residue |
A | THR247 |
A | VAL337 |
A | LYS338 |
A | HOH594 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 487 |
Chain | Residue |
A | MSE314 |
A | HOH515 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 488 |
Chain | Residue |
A | LYS281 |
A | ARG285 |
A | TYR327 |
B | ASP411 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 489 |
Chain | Residue |
A | PRO102 |
A | ASN103 |
A | GLU104 |
A | ALA105 |
A | HOH500 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG A 490 |
Chain | Residue |
A | LYS338 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 491 |
Chain | Residue |
A | GLU25 |
A | GLY26 |
A | LYS28 |
A | ARG92 |
A | ASN103 |
A | GLY106 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 492 |
Chain | Residue |
A | PHE301 |
A | THR304 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 493 |
Chain | Residue |
A | TYR66 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 494 |
Chain | Residue |
A | LYS338 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 495 |
Chain | Residue |
A | ASP397 |
A | LYS404 |
site_id | CC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT A 496 |
Chain | Residue |
A | TYR394 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FMT A 497 |
Chain | Residue |
A | ARG322 |
A | GLU323 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 478 |
Chain | Residue |
B | TRP349 |
B | SER430 |
B | ALA431 |
B | GLY432 |
B | LYS438 |
B | TYR440 |
B | HOH558 |
B | HOH605 |
B | HOH702 |
B | HOH743 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 479 |
Chain | Residue |
B | ARG295 |
B | LYS298 |
B | HOH540 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 B 480 |
Chain | Residue |
B | ARG437 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG B 481 |
Chain | Residue |
B | PHE292 |
B | GLU294 |
B | LYS297 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG B 482 |
Chain | Residue |
B | ASN7 |
B | LEU417 |
B | MSE418 |
site_id | CC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG B 483 |
Chain | Residue |
B | ASP348 |
B | TRP349 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG B 484 |
Chain | Residue |
B | PHE301 |
B | THR304 |
B | HOH491 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 485 |
Chain | Residue |
B | ALA344 |
B | PHE378 |
B | HOH670 |
B | HOH711 |
B | HOH735 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 486 |
Chain | Residue |
B | PHE81 |
B | LYS82 |
B | TYR120 |
B | GLY121 |
B | HOH684 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 487 |
Chain | Residue |
B | GLY42 |
B | VAL43 |
B | THR433 |
B | HOH559 |
site_id | DC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT B 488 |
Chain | Residue |
B | PRO340 |
site_id | DC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE FMT B 489 |
Chain | Residue |
B | ASP346 |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFIVENGFG |
Chain | Residue | Details |
A | LEU371-GLY379 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGgAvAAHQlEgG |
Chain | Residue | Details |
A | PHE8-GLY22 |