1J9Y
Crystal structure of mannanase 26A from Pseudomonas cellulosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0006080 | biological_process | substituted mannan metabolic process |
| A | 0010391 | biological_process | glucomannan metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016985 | molecular_function | mannan endo-1,4-beta-mannosidase activity |
| A | 0051069 | biological_process | galactomannan metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | HIS71 |
| A | GLU239 |
| A | HOH1109 |
| A | HOH1278 |
| A | HOH1335 |
| A | HOH1413 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | HOH1203 |
| A | HOH1225 |
| A | HOH1347 |
| A | ASP222 |
| A | HOH1123 |
| A | HOH1199 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1003 |
| Chain | Residue |
| A | HIS79 |
| A | ASP111 |
| A | GLU121 |
| A | HOH1542 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1004 |
| Chain | Residue |
| A | ARG208 |
| A | HIS211 |
| A | ASP283 |
| A | GLU320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:12203498, ECO:0000305|PubMed:12841226, ECO:0000305|PubMed:19441796, ECO:0000305|PubMed:8973192 |
| Chain | Residue | Details |
| A | GLU212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:12203498, ECO:0000305|PubMed:8973192 |
| Chain | Residue | Details |
| A | GLU320 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12203498, ECO:0000269|PubMed:12841226 |
| Chain | Residue | Details |
| A | GLU121 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12203498, ECO:0000269|PubMed:12841226, ECO:0000269|PubMed:19441796 |
| Chain | Residue | Details |
| A | HIS377 | |
| A | HIS143 | |
| A | TRP360 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12203498, ECO:0000305|PubMed:11382747 |
| Chain | Residue | Details |
| A | TRP162 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11382747 |
| Chain | Residue | Details |
| A | TRP217 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12841226, ECO:0000269|PubMed:19441796 |
| Chain | Residue | Details |
| A | TYR285 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | SITE: Plays an important role in maintaining the position of the catalytic nucleophile => ECO:0000269|PubMed:11382747, ECO:0000305|PubMed:12203498 |
| Chain | Residue | Details |
| A | HIS211 |
