5N6N
CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX
Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0004555 | molecular_function | alpha,alpha-trehalase activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0005991 | biological_process | trehalose metabolic process |
C | 0005993 | biological_process | trehalose catabolic process |
C | 0015927 | molecular_function | trehalase activity |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0046872 | molecular_function | metal ion binding |
C | 0071465 | biological_process | cellular response to desiccation |
Functional Information from PROSITE/UniProt
site_id | PS00796 |
Number of Residues | 11 |
Details | 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV |
Chain | Residue | Details |
A | ARG43-VAL53 |
site_id | PS00797 |
Number of Residues | 20 |
Details | 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS |
Chain | Residue | Details |
A | TYR216-SER235 |
site_id | PS00927 |
Number of Residues | 14 |
Details | TREHALASE_1 Trehalase signature 1. PGGRFnElYgWDsY |
Chain | Residue | Details |
C | PRO299-TYR312 |
site_id | PS00928 |
Number of Residues | 10 |
Details | TREHALASE_2 Trehalase signature 2. QWDyPfGWAP |
Chain | Residue | Details |
C | GLN623-PRO632 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:29087344, ECO:0007744|PDB:5M4A |
Chain | Residue | Details |
C | ASP478 | |
C | GLU674 | |
B | GLU136 | |
B | GLU185 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5N6N |
Chain | Residue | Details |
C | ASP114 | |
C | ASP116 | |
C | ASN118 | |
C | GLN120 | |
C | ASP125 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13482 |
Chain | Residue | Details |
C | ARG302 | |
B | SER89 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5M4A, ECO:0007744|PDB:5N6N |
Chain | Residue | Details |
C | TRP309 | |
C | ASN346 | |
C | ARG355 | |
C | GLU424 | |
C | ARG473 | |
C | GLY476 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: BMH1 binding => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5N6N |
Chain | Residue | Details |
C | ARG55 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
C | SER2 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SER20 | |
C | SER21 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SER23 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | THR58 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SEP60 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SER66 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
C | SEP83 |