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7PZ7

Structure of an LPMO at 1.13x10^6 Gy

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005576cellular_componentextracellular region
A0008810molecular_functioncellulase activity
A0030245biological_processcellulose catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:35204695, ECO:0000269|PubMed:36071795, ECO:0000269|DOI:10.3390/catal12020139, ECO:0007744|PDB:2YET, ECO:0007744|PDB:3ZUD, ECO:0007744|PDB:7PU1, ECO:0007744|PDB:7PZ3, ECO:0007744|PDB:7PZ4, ECO:0007744|PDB:7PZ5, ECO:0007744|PDB:7PZ6, ECO:0007744|PDB:7PZ7, ECO:0007744|PDB:7PZ8, ECO:0007744|PDB:7Q1K
ChainResidueDetails
AHIC1
AHIS86

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6
ChainResidueDetails
AHIS164
AGLN173
ATYR175

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Methylhistidine => ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843
ChainResidueDetails
AHIC1

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21876164, ECO:0000269|DOI:10.3390/catal12020139, ECO:0007744|PDB:2YET, ECO:0007744|PDB:3ZUD, ECO:0007744|PDB:7Q1K
ChainResidueDetails
AASN138

226707

PDB entries from 2024-10-30

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