3VSF
Crystal structure of 1,3Gal43A, an exo-beta-1,3-Galactanase from Clostridium thermocellum
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 |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
E | 0005975 | biological_process | carbohydrate metabolic process |
F | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
F | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | ASP463 |
A | VAL464 |
A | LYS466 |
A | GLN476 |
A | TRP478 |
A | ASN485 |
A | GLN486 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | TYR431 |
A | ASN434 |
A | ASN438 |
A | ASP416 |
A | ASP419 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 601 |
Chain | Residue |
B | ASN275 |
B | TYR279 |
B | ARG280 |
B | TYR334 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 602 |
Chain | Residue |
B | ASP463 |
B | VAL464 |
B | ARG465 |
B | LYS466 |
B | TRP467 |
B | GLN476 |
B | TRP478 |
B | ASN485 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 601 |
Chain | Residue |
C | ASP463 |
C | LYS466 |
C | GLN476 |
C | TRP478 |
C | ASN485 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 602 |
Chain | Residue |
C | ASP416 |
C | LYS418 |
C | ASP419 |
C | GLU420 |
C | TYR431 |
C | ASN434 |
C | ASN438 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 603 |
Chain | Residue |
C | ASN275 |
C | THR277 |
C | TYR279 |
C | TYR334 |
C | HOH706 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 604 |
Chain | Residue |
A | LYS466 |
C | GLU112 |
C | ARG113 |
C | ASP180 |
C | TRP250 |
C | GLN282 |
C | HOH709 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 601 |
Chain | Residue |
D | ASN275 |
D | THR277 |
D | TYR279 |
D | ARG280 |
D | ARG303 |
D | TYR334 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 601 |
Chain | Residue |
E | ASP463 |
E | VAL464 |
E | ARG465 |
E | LYS466 |
E | GLN476 |
E | TRP478 |
E | ASN485 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL F 601 |
Chain | Residue |
F | ASP416 |
F | ASP419 |
F | GLU420 |
F | TYR431 |
F | ASN434 |
F | ASN438 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL F 602 |
Chain | Residue |
F | ASP463 |
F | VAL464 |
F | ARG465 |
F | LYS466 |
F | GLN476 |
F | TRP478 |
F | ASN485 |
F | GLN486 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL F 603 |
Chain | Residue |
F | GLU112 |
F | ARG113 |
F | TYR137 |
F | ASP180 |
F | GLU229 |
F | GLN282 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL F 604 |
Chain | Residue |
F | LYS221 |
F | LEU222 |
F | PHE223 |
F | SER265 |
F | GLY266 |
F | TRP267 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LASGWSQLYNLGNST |
Chain | Residue | Details |
A | LEU263-THR277 |