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5TKG

Neurospora crassa polysaccharide monooxygenase 2 resting state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0019825molecular_functionoxygen binding
A0030245biological_processcellulose catabolic process
A0046872molecular_functionmetal ion binding
A0071999biological_processextracellular polysaccharide catabolic process
B0004497molecular_functionmonooxygenase activity
B0005507molecular_functioncopper ion binding
B0005576cellular_componentextracellular region
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0019825molecular_functionoxygen binding
B0030245biological_processcellulose catabolic process
B0046872molecular_functionmetal ion binding
B0071999biological_processextracellular polysaccharide catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:36507176
ChainResidueDetails
AHIS157
BHIS157

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22578542, ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28177316, ECO:0000269|PubMed:36507176, ECO:0007744|PDB:4EIR, ECO:0007744|PDB:5TKF, ECO:0007744|PDB:5TKG, ECO:0007744|PDB:5TKH, ECO:0007744|PDB:5TKI, ECO:0007744|PDB:7T5C, ECO:0007744|PDB:7T5D, ECO:0007744|PDB:7T5E
ChainResidueDetails
AHIS1
AHIS84
BHIS1
BHIS84

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28177316, ECO:0000269|PubMed:36507176, ECO:0007744|PDB:5TKG, ECO:0007744|PDB:5TKH, ECO:0007744|PDB:7T5D
ChainResidueDetails
AGLU30
BGLU30

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28177316, ECO:0000269|PubMed:36507176, ECO:0007744|PDB:5TKF, ECO:0007744|PDB:5TKG, ECO:0007744|PDB:5TKH, ECO:0007744|PDB:7T5D
ChainResidueDetails
AHIS157
AGLN166
BHIS157
BGLN166

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28177316, ECO:0000269|PubMed:36507176, ECO:0007744|PDB:5TKF, ECO:0007744|PDB:5TKG, ECO:0007744|PDB:5TKH, ECO:0007744|PDB:5TKI, ECO:0007744|PDB:7T5C, ECO:0007744|PDB:7T5D, ECO:0007744|PDB:7T5E
ChainResidueDetails
ATYR168
BTYR168

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Promotes oxygen activation => ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28291519
ChainResidueDetails
AHIS157
BHIS157

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:22578542, ECO:0000269|PubMed:28004877, ECO:0000269|PubMed:28177316, ECO:0000269|PubMed:36507176, ECO:0007744|PDB:4EIR, ECO:0007744|PDB:5TKF, ECO:0007744|PDB:5TKG, ECO:0007744|PDB:5TKH, ECO:0007744|PDB:5TKI, ECO:0007744|PDB:7T5C, ECO:0007744|PDB:7T5D, ECO:0007744|PDB:7T5E
ChainResidueDetails
AASN60
BASN60

219140

PDB entries from 2024-05-01

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