2CB1

Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003961	molecular_function	O-acetylhomoserine aminocarboxypropyltransferase activity
A	0004124	molecular_function	cysteine synthase activity
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0006535	biological_process	cysteine biosynthetic process from serine
A	0008652	biological_process	amino acid biosynthetic process
A	0009086	biological_process	methionine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
A	0051009	molecular_function	O-acetylhomoserine sulfhydrylase activity
A	0071266	biological_process	'de novo' L-methionine biosynthetic process
A	0071269	biological_process	L-homocysteine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP A 1202

Chain	Residue
A	TYR50
A	THR201
A	LYS202
A	GLY212
A	ARG52
A	SER79
A	GLY80
A	GLN81
A	PHE105
A	ASP176
A	THR178
A	SER199

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|Ref.3, ECO:0007744|PDB:2CB1

Chain	Residue	Details
A	LYS202

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE105
A	ASP176

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	ARG52

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