6YDC

X-ray structure of LPMO

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005576	cellular_component	extracellular region
A	0030245	biological_process	cellulose catabolic process
A	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005576	cellular_component	extracellular region
B	0030245	biological_process	cellulose catabolic process
B	0046872	molecular_function	metal ion binding
C	0004497	molecular_function	monooxygenase activity
C	0005576	cellular_component	extracellular region
C	0030245	biological_process	cellulose catabolic process
C	0046872	molecular_function	metal ion binding
D	0004497	molecular_function	monooxygenase activity
D	0005576	cellular_component	extracellular region
D	0030245	biological_process	cellulose catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
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	HIC1
D	HIC1
D	HIS79
D	TYR169
A	HIS79
A	TYR169
B	HIC1
B	HIS79
B	TYR169
C	HIC1
C	HIS79
C	TYR169

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDE

Chain	Residue	Details
A	GLY45
B	GLY45
C	GLY45
D	GLY45

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE

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

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6

Chain	Residue	Details
A	HIS152
B	HIS152
C	HIS152
D	HIS152

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