5NIT
Glucose oxidase mutant A2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0046562 | molecular_function | beta-D-glucose oxidase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PROSITE/UniProt
site_id | PS00623 |
Number of Residues | 24 |
Details | GMC_OXRED_1 GMC oxidoreductases signature 1. GNgLGGSTlVNggtWtrPhkaqvD |
Chain | Residue | Details |
A | GLY97-ASP120 |
site_id | PS00624 |
Number of Residues | 15 |
Details | GMC_OXRED_2 GMC oxidoreductases signature 2. GSavSPtILeySGIG |
Chain | Residue | Details |
A | GLY290-GLY304 |
site_id | PS00626 |
Number of Residues | 11 |
Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. FGCGdPHGVSM |
Chain | Residue | Details |
A | PHE204-MET214 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1GAL |
Chain | Residue | Details |
A | HIS516 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | LEU29 | |
A | GLU50 | |
A | SER103 | |
A | ASN107 | |
A | THR110 | |
A | VAL250 | |
A | GLY549 | |
A | MET561 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR |
Chain | Residue | Details |
A | VAL30 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, ECO:0007744|PDB:1CF3, ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | GLY108 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29291138, ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | LYS537 | |
A | VAL538 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN43 | |
A | ASN89 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:10216293, ECO:0000269|PubMed:21568312, ECO:0000269|PubMed:29291138, ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1CF3, ECO:0007744|PDB:1GAL, ECO:0007744|PDB:3QVP, ECO:0007744|PDB:3QVR, ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | ASN161 | |
A | ASN355 | |
A | ASN388 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29291138, ECO:0007744|PDB:1GAL |
Chain | Residue | Details |
A | ASN168 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29291138, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | ASN258 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0007744|PDB:5NIW |
Chain | Residue | Details |
A | ASN473 |
Catalytic Information from CSA