1QNQ
The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5
Functional Information from GO Data
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10666621 |
Chain | Residue | Details |
A | GLU169 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10666621 |
Chain | Residue | Details |
A | GLU276 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10666621, ECO:0007744|PDB:1QNR |
Chain | Residue | Details |
A | GLU169 | |
A | GLU205 | |
A | TRP247 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for transglycosylation activity => ECO:0000269|DOI:10.3109/10242422.2012.674726 |
Chain | Residue | Details |
A | ARG171 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10666621, ECO:0007744|PDB:1QNO, ECO:0007744|PDB:1QNP, ECO:0007744|PDB:1QNQ |
Chain | Residue | Details |
A | ASN130 | |
A | ASN157 | |
A | ASN250 | |
A | ASN328 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
A | TYR243 | |
A | GLU276 | |
A | GLU169 | |
A | HIS241 | |
A | ASN168 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
A | ARG54 | |
A | GLU276 | |
A | GLU169 |