4YK7

Crystal structure of S-hydroxynitrile lyase from Manihot esculenta (His103Leu)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016829	molecular_function	lyase activity
A	0047606	molecular_function	(S)-hydroxynitrile lyase activity
A	0052891	molecular_function	aliphatic (S)-hydroxynitrile lyase activity
A	0052892	molecular_function	aromatic (S)-hydroxynitrile lyase activity
B	0016829	molecular_function	lyase activity
B	0047606	molecular_function	(S)-hydroxynitrile lyase activity
B	0052891	molecular_function	aliphatic (S)-hydroxynitrile lyase activity
B	0052892	molecular_function	aromatic (S)-hydroxynitrile lyase activity
C	0016829	molecular_function	lyase activity
C	0047606	molecular_function	(S)-hydroxynitrile lyase activity
C	0052891	molecular_function	aliphatic (S)-hydroxynitrile lyase activity
C	0052892	molecular_function	aromatic (S)-hydroxynitrile lyase activity
D	0016829	molecular_function	lyase activity
D	0047606	molecular_function	(S)-hydroxynitrile lyase activity
D	0052891	molecular_function	aliphatic (S)-hydroxynitrile lyase activity
D	0052892	molecular_function	aromatic (S)-hydroxynitrile lyase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:11173464, ECO:0000305|PubMed:11316882

Chain	Residue	Details
A	SER80
A	HIS236
B	SER80
B	HIS236
C	SER80
C	HIS236
D	SER80
D	HIS236

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:11173464, ECO:0007744|PDB:1DWO

Chain	Residue	Details
A	THR11
D	THR11
D	SER80
D	CYS81
A	SER80
A	CYS81
B	THR11
B	SER80
B	CYS81
C	THR11
C	SER80
C	CYS81

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site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Increases basicity of active site His => ECO:0000305|PubMed:11316882

Chain	Residue	Details
A	ASP208
B	ASP208
C	ASP208
D	ASP208

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