4PVA

Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0045493	biological_process	xylan catabolic process
A	0046373	biological_process	L-arabinose metabolic process
A	0046556	molecular_function	alpha-L-arabinofuranosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 501

Chain	Residue
A	VAL35
A	HOH753
A	SER36
A	LEU219
A	GLY271
A	GLN272
A	TRP273
A	GLY294
A	HOH642
A	HOH726

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
A	ARG108
A	GLU117
A	LYS120
A	ASN128
A	HOH727
A	HOH743
A	HOH885
A	HOH927
A	HOH999

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site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 503

Chain	Residue
A	ARG48
A	ILE50
A	LYS73
A	ASP99
A	HOH737
A	HOH764
A	HOH1056
A	HOH1095
A	HOH1104
A	HOH1108

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 504

Chain	Residue
A	ASP178
A	ARG236
A	GLU241
A	HOH1042

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site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 505

Chain	Residue
A	LYS54
A	GLU230
A	ARG259
A	HIS303
A	GLN328
A	TYR338
A	HOH624
A	HOH672
A	HOH747
A	HOH857

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 506

Chain	Residue
A	ASP177
A	HIS188
A	ARG268
A	ILE269
A	ASP270
A	HOH611

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