5OYN

Crystal structure of D-xylonate dehydratase in holo-form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0042732	biological_process	D-xylose metabolic process
A	0042843	biological_process	D-xylose catabolic process
A	0046872	molecular_function	metal ion binding
A	0047929	molecular_function	gluconate dehydratase activity
A	0050401	molecular_function	xylonate dehydratase activity
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0042732	biological_process	D-xylose metabolic process
B	0042843	biological_process	D-xylose catabolic process
B	0046872	molecular_function	metal ion binding
B	0047929	molecular_function	gluconate dehydratase activity
B	0050401	molecular_function	xylonate dehydratase activity
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0042732	biological_process	D-xylose metabolic process
C	0042843	biological_process	D-xylose catabolic process
C	0046872	molecular_function	metal ion binding
C	0047929	molecular_function	gluconate dehydratase activity
C	0050401	molecular_function	xylonate dehydratase activity
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0003824	molecular_function	catalytic activity
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0042732	biological_process	D-xylose metabolic process
D	0042843	biological_process	D-xylose catabolic process
D	0046872	molecular_function	metal ion binding
D	0047929	molecular_function	gluconate dehydratase activity
D	0050401	molecular_function	xylonate dehydratase activity
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 601

Chain	Residue
A	GLU92
A	ASP129
A	KCX130
A	GLU463
A	HOH718

---

site_id	AC2
Number of Residues	5
Details	binding site for residue FES A 602

Chain	Residue
B	ARG30
A	CYS60
A	ASN93
A	CYS128
A	CYS201

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MG B 601

Chain	Residue
B	GLU92
B	ASP129
B	KCX130
B	THR206
B	GLU463
B	HOH714

---

site_id	AC4
Number of Residues	7
Details	binding site for residue FES B 602

Chain	Residue
A	ARG30
B	CYS60
B	ASN93
B	CYS128
B	ASP129
B	HIS200
B	CYS201

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG C 601

Chain	Residue
C	GLU92
C	ASP129
C	KCX130
C	GLU463
C	HOH726

---

site_id	AC6
Number of Residues	5
Details	binding site for residue FES C 602

Chain	Residue
C	CYS60
C	CYS128
C	ASP129
C	HIS200
C	CYS201

---

site_id	AC7
Number of Residues	5
Details	binding site for residue MG D 601

Chain	Residue
D	GLU92
D	ASP129
D	KCX130
D	GLU463
D	HOH711

---

site_id	AC8
Number of Residues	7
Details	binding site for residue FES D 602

Chain	Residue
C	ARG30
D	CYS60
D	ASN93
D	CYS128
D	ASP129
D	CYS201
D	HOH764

---

Functional Information from PROSITE/UniProt

site_id	PS00886
Number of Residues	11
Details	ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKttPAgimA

Chain	Residue	Details
A	CYS128-ALA138

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:29339766

Chain	Residue	Details
A	CYS60
B	ASP129
B	CYS201
B	GLU463
C	CYS60
C	GLU92
C	CYS128
C	ASP129
C	CYS201
C	GLU463
D	CYS60
A	GLU92
D	GLU92
D	CYS128
D	ASP129
D	CYS201
D	GLU463
A	CYS128
A	ASP129
A	CYS201
A	GLU463
B	CYS60
B	GLU92
B	CYS128

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