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 | 0005976 | biological_process | polysaccharide metabolic process |
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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8973192","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8973192","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12841226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19441796","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Site: {"description":"Plays an important role in maintaining the position of the catalytic nucleophile","evidences":[{"source":"PubMed","id":"11382747","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12203498","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |