1R7O
Crystal Structure of apo-mannanase 26A from Psudomonas 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 | GLU67 |
| A | HIS71 |
| A | GLU239 |
| A | HOH2108 |
| A | HOH2270 |
| A | HOH2387 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | HOH2196 |
| A | HOH2218 |
| A | HOH2329 |
| A | ASP222 |
| A | HOH2121 |
| A | HOH2192 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1003 |
| Chain | Residue |
| A | HIS79 |
| A | ASP111 |
| A | GLU121 |
| A | HOH2501 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1004 |
| Chain | Residue |
| A | ARG208 |
| A | HIS211 |
| A | GLU212 |
| A | ASP283 |
| A | GLU320 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
| Chain | Residue |
| A | PHE259 |
| A | TRP260 |
| A | ASP261 |
| A | HOH2341 |
| A | HOH2377 |
| A | HOH2494 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 2002 |
| Chain | Residue |
| A | TYR132 |
| A | ALA133 |
| A | GLU198 |
| A | GLN199 |
| A | TYR415 |
| A | GLN416 |
| A | HOH2055 |
| A | HOH2379 |
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 | HIS143 | |
| A | TRP360 | |
| A | HIS377 |
| 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 |
