2Q3C

2.1 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) Holoenzyme From MYCOBACTERIUM TUBERCULOSIS in Complex with the Inhibitory Peptide DFSI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004122	molecular_function	cystathionine beta-synthase activity
A	0004124	molecular_function	cysteine synthase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006535	biological_process	cysteine biosynthetic process from serine
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0019344	biological_process	cysteine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0080146	molecular_function	L-cysteine desulfhydrase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 311

Chain	Residue
A	VAL263
A	TYR299
A	HOH360

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Functional Information from PROSITE/UniProt

site_id	PS00901
Number of Residues	19
Details	CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEffn.PAnSVKdRiGvaM

Chain	Residue	Details
A	LYS33-MET51

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:17567578

Chain	Residue	Details
A	ASN74
A	GLY178
A	SER266

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17567578

Chain	Residue	Details
A	LLP44

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