1HN0

CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0006027	biological_process	glycosaminoglycan catabolic process
A	0016829	molecular_function	lyase activity
A	0030246	molecular_function	carbohydrate binding
A	0034000	molecular_function	chondroitin-sulfate-ABC endolyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1800

Chain	Residue
A	HIS43
A	MET70
A	GLN73
A	ASP211
A	HOH2159

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15691229, ECO:0000269|PubMed:16108757

Chain	Residue	Details
A	HIS501

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255

Chain	Residue	Details
A	TYR508

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12706721, ECO:0007744|PDB:1HN0

Chain	Residue	Details
A	HIS43
A	MET70
A	GLN73
A	ASP211

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000255

Chain	Residue	Details
A	ARG560

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Important for catalytic activity

Chain	Residue	Details
A	GLU653

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1cb8

Chain	Residue	Details
A	TYR508
A	ARG560
A	HIS501

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