4D8U

Crystal structure of D-Cysteine desulfhydrase from Salmonella typhimurium at 3.3 A in monoclinic space group with 8 subunits in the asymmetric unit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0019148	molecular_function	D-cysteine desulfhydrase activity
A	0046416	biological_process	D-amino acid metabolic process
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0019148	molecular_function	D-cysteine desulfhydrase activity
B	0046416	biological_process	D-amino acid metabolic process
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0019148	molecular_function	D-cysteine desulfhydrase activity
C	0046416	biological_process	D-amino acid metabolic process
D	0003824	molecular_function	catalytic activity
D	0016829	molecular_function	lyase activity
D	0019148	molecular_function	D-cysteine desulfhydrase activity
D	0046416	biological_process	D-amino acid metabolic process
E	0003824	molecular_function	catalytic activity
E	0016829	molecular_function	lyase activity
E	0019148	molecular_function	D-cysteine desulfhydrase activity
E	0046416	biological_process	D-amino acid metabolic process
F	0003824	molecular_function	catalytic activity
F	0016829	molecular_function	lyase activity
F	0019148	molecular_function	D-cysteine desulfhydrase activity
F	0046416	biological_process	D-amino acid metabolic process
G	0003824	molecular_function	catalytic activity
G	0016829	molecular_function	lyase activity
G	0019148	molecular_function	D-cysteine desulfhydrase activity
G	0046416	biological_process	D-amino acid metabolic process
H	0003824	molecular_function	catalytic activity
H	0016829	molecular_function	lyase activity
H	0019148	molecular_function	D-cysteine desulfhydrase activity
H	0046416	biological_process	D-amino acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	LLP51
A	SER78
A	ASN79
A	HIS80
A	TYR261
A	TYR287

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	HIS80
B	GLY159
B	TYR261
B	TYR287
B	LLP51
B	SER78
B	ASN79

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 401

Chain	Residue
C	LLP51
C	SER78
C	ASN79
C	HIS80
C	GLY159
C	TYR261
C	TYR287

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 401

Chain	Residue
D	LLP51
D	SER78
D	ASN79
D	HIS80
D	TYR261
D	TYR287

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 401

Chain	Residue
E	LLP51
E	SER78
E	ASN79
E	HIS80
E	TYR261
E	TYR287

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 F 401

Chain	Residue
F	LLP51
F	SER78
F	ASN79
F	HIS80
F	TYR261
F	TYR287

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 G 401

Chain	Residue
G	LLP51
G	SER78
G	ASN79
G	HIS80
G	TYR261
G	TYR287

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 H 401

Chain	Residue
H	LLP51
H	SER78
H	ASN79
H	HIS80
H	TYR261
H	TYR287

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01045

Chain	Residue	Details
A	LLP51
B	LLP51
C	LLP51
D	LLP51
E	LLP51
F	LLP51
G	LLP51
H	LLP51

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