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5NIT

Glucose oxidase mutant A2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0046562molecular_functionbeta-D-glucose oxidase activity
A0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GNgLGGSTlVNggtWtrPhkaqvD
ChainResidueDetails
AGLY97-ASP120

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GSavSPtILeySGIG
ChainResidueDetails
AGLY290-GLY304

site_idPS00626
Number of Residues11
DetailsRCC1_2 Regulator of chromosome condensation (RCC1) signature 2. FGCGdPHGVSM
ChainResidueDetails
APHE204-MET214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8421298, ECO:0007744|PDB:1GAL
ChainResidueDetails
AHIS516

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: 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
ChainResidueDetails
ALEU29
AGLU50
ASER103
AASN107
ATHR110
AVAL250
AGLY549
AMET561

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AVAL30

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AGLY108

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:29291138, ECO:0007744|PDB:5NIT, ECO:0007744|PDB:5NIW
ChainResidueDetails
ALYS537
AVAL538

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN43
AASN89

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: 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
ChainResidueDetails
AASN161
AASN355
AASN388

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29291138, ECO:0007744|PDB:1GAL
ChainResidueDetails
AASN168

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29291138, ECO:0007744|PDB:5NIW
ChainResidueDetails
AASN258

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0007744|PDB:5NIW
ChainResidueDetails
AASN473

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 567
ChainResidueDetails
AHIS516proton acceptor

237735

PDB entries from 2025-06-18

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