Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5J84

Crystal structure of L-arabinonate dehydratase in holo-form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008869	molecular_function	galactonate dehydratase activity
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0019568	biological_process	arabinose catabolic process
A	0046872	molecular_function	metal ion binding
A	0047818	molecular_function	D-fuconate dehydratase activity
A	0050020	molecular_function	L-arabinonate dehydratase activity
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0008869	molecular_function	galactonate dehydratase activity
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0019568	biological_process	arabinose catabolic process
B	0046872	molecular_function	metal ion binding
B	0047818	molecular_function	D-fuconate dehydratase activity
B	0050020	molecular_function	L-arabinonate dehydratase activity
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0008869	molecular_function	galactonate dehydratase activity
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0019568	biological_process	arabinose catabolic process
C	0046872	molecular_function	metal ion binding
C	0047818	molecular_function	D-fuconate dehydratase activity
C	0050020	molecular_function	L-arabinonate dehydratase activity
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0008869	molecular_function	galactonate dehydratase activity
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0019568	biological_process	arabinose catabolic process
D	0046872	molecular_function	metal ion binding
D	0047818	molecular_function	D-fuconate dehydratase activity
D	0050020	molecular_function	L-arabinonate dehydratase activity
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0008869	molecular_function	galactonate dehydratase activity
E	0016829	molecular_function	lyase activity
E	0016836	molecular_function	hydro-lyase activity
E	0019568	biological_process	arabinose catabolic process
E	0046872	molecular_function	metal ion binding
E	0047818	molecular_function	D-fuconate dehydratase activity
E	0050020	molecular_function	L-arabinonate dehydratase activity
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0008869	molecular_function	galactonate dehydratase activity
F	0016829	molecular_function	lyase activity
F	0016836	molecular_function	hydro-lyase activity
F	0019568	biological_process	arabinose catabolic process
F	0046872	molecular_function	metal ion binding
F	0047818	molecular_function	D-fuconate dehydratase activity
F	0050020	molecular_function	L-arabinonate dehydratase activity
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
G	0008869	molecular_function	galactonate dehydratase activity
G	0016829	molecular_function	lyase activity
G	0016836	molecular_function	hydro-lyase activity
G	0019568	biological_process	arabinose catabolic process
G	0046872	molecular_function	metal ion binding
G	0047818	molecular_function	D-fuconate dehydratase activity
G	0050020	molecular_function	L-arabinonate dehydratase activity
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0008869	molecular_function	galactonate dehydratase activity
H	0016829	molecular_function	lyase activity
H	0016836	molecular_function	hydro-lyase activity
H	0019568	biological_process	arabinose catabolic process
H	0046872	molecular_function	metal ion binding
H	0047818	molecular_function	D-fuconate dehydratase activity
H	0050020	molecular_function	L-arabinonate dehydratase activity
H	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	GLU91
A	ASP128
A	KCX129
A	GLU453
A	HOH769

site_id	AC2
Number of Residues	8
Details	binding site for residue FES A 602

Chain	Residue
A	THR199
A	CYS200
A	ALA206
B	TYR26
A	CYS59
A	ASN92
A	CYS127
A	ASP128

site_id	AC3
Number of Residues	7
Details	binding site for residue MG B 601

Chain	Residue
B	GLU91
B	ASP128
B	KCX129
B	THR205
B	ASN278
B	GLU453
B	HOH814

site_id	AC4
Number of Residues	8
Details	binding site for residue FES B 602

Chain	Residue
A	TYR26
A	TRP30
B	CYS59
B	ASN92
B	CYS127
B	ASP128
B	CYS200
B	HOH838

site_id	AC5
Number of Residues	7
Details	binding site for residue MG C 601

Chain	Residue
C	GLU91
C	ASP128
C	KCX129
C	THR205
C	ASN278
C	GLU453
C	HOH719

site_id	AC6
Number of Residues	6
Details	binding site for residue FES C 602

Chain	Residue
C	CYS59
C	CYS127
C	THR199
C	CYS200
D	TYR26
D	TRP30

site_id	AC7
Number of Residues	6
Details	binding site for residue MG D 601

Chain	Residue
D	GLU91
D	ASP128
D	KCX129
D	THR205
D	GLU453
D	HOH816

site_id	AC8
Number of Residues	5
Details	binding site for residue FES D 602

Chain	Residue
C	TRP30
D	CYS59
D	CYS127
D	ASP128
D	CYS200

site_id	AC9
Number of Residues	7
Details	binding site for residue MG E 601

Chain	Residue
E	GLU91
E	ASP128
E	KCX129
E	THR205
E	GLU453
E	HOH785
E	HOH790

site_id	AD1
Number of Residues	7
Details	binding site for residue FES E 602

Chain	Residue
E	CYS59
E	ASN92
E	CYS127
E	ASP128
E	CYS200
F	TYR26
F	TRP30

site_id	AD2
Number of Residues	6
Details	binding site for residue MG F 601

Chain	Residue
F	GLU91
F	ASP128
F	KCX129
F	GLU453
F	HOH729
F	HOH758

site_id	AD3
Number of Residues	8
Details	binding site for residue FES F 602

Chain	Residue
E	TRP30
F	CYS59
F	ASN92
F	CYS127
F	ASP128
F	THR199
F	CYS200
F	ALA206

site_id	AD4
Number of Residues	5
Details	binding site for residue MG G 601

Chain	Residue
G	GLU91
G	ASP128
G	KCX129
G	GLU453
G	HOH788

site_id	AD5
Number of Residues	8
Details	binding site for residue FES G 602

Chain	Residue
G	CYS59
G	ASN92
G	CYS127
G	ASP128
G	CYS200
G	ALA206
H	TYR26
H	TRP30

site_id	AD6
Number of Residues	6
Details	binding site for residue MG H 601

Chain	Residue
H	GLU91
H	ASP128
H	KCX129
H	GLU453
H	HOH715
H	HOH787

site_id	AD7
Number of Residues	6
Details	binding site for residue FES H 602

Chain	Residue
G	TYR26
H	CYS59
H	ASN92
H	CYS127
H	ASP128
H	CYS200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:28574691

Chain	Residue	Details
A	CYS59
B	ASP128
B	CYS200
B	GLU453
C	CYS59
C	GLU91
C	CYS127
C	ASP128
C	CYS200
C	GLU453
D	CYS59
A	GLU91
D	GLU91
D	CYS127
D	ASP128
D	CYS200
D	GLU453
E	CYS59
E	GLU91
E	CYS127
E	ASP128
E	CYS200
A	CYS127
E	GLU453
F	CYS59
F	GLU91
F	CYS127
F	ASP128
F	CYS200
F	GLU453
G	CYS59
G	GLU91
G	CYS127
A	ASP128
G	ASP128
G	CYS200
G	GLU453
H	CYS59
H	GLU91
H	CYS127
H	ASP128
H	CYS200
H	GLU453
A	CYS200
A	GLU453
B	CYS59
B	GLU91
B	CYS127

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)