7PZ8

Structure of an LPMO at 3.12x10^6 Gy

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005576	cellular_component	extracellular region
A	0008810	molecular_function	cellulase activity
A	0030245	biological_process	cellulose catabolic process
A	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: 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

Chain	Residue	Details
A	HIC1
A	HIS86

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6

Chain	Residue	Details
A	HIS164
A	GLN173
A	TYR175

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Methylhistidine => ECO:0000269|PubMed:21876164, ECO:0000269|PubMed:29971843

Chain	Residue	Details
A	HIC1

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN138

---