6YDD

X-ray structure of LPMO.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004497	molecular_function	monooxygenase activity
A	0005576	cellular_component	extracellular region
A	0016491	molecular_function	oxidoreductase activity
A	0030245	biological_process	cellulose catabolic process
A	0046872	molecular_function	metal ion binding
B	0000272	biological_process	polysaccharide catabolic process
B	0004497	molecular_function	monooxygenase activity
B	0005576	cellular_component	extracellular region
B	0016491	molecular_function	oxidoreductase activity
B	0030245	biological_process	cellulose catabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0007744|PDB:5NLT, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE, ECO:0007744|PDB:6YDF

Chain	Residue	Details
A	HIC306
A	HIS79
A	TYR169
B	HIC304
B	HIS79
B	TYR169

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDE

Chain	Residue	Details
A	GLY45
B	GLY45

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE

Chain	Residue	Details
A	ASP76
A	SER78
A	ASP155
B	ASP76
B	SER78
B	ASP155

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6

Chain	Residue	Details
A	HIS152
B	HIS152

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