Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QKE

Crystal structure of D-mannonate dehydratase from Chromohalobacter Salexigens complexed with Mg and D-Gluconate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008927	molecular_function	mannonate dehydratase activity
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0047929	molecular_function	gluconate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0008927	molecular_function	mannonate dehydratase activity
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0047929	molecular_function	gluconate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0008927	molecular_function	mannonate dehydratase activity
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
C	0047929	molecular_function	gluconate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0008927	molecular_function	mannonate dehydratase activity
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
D	0047929	molecular_function	gluconate dehydratase activity
E	0000287	molecular_function	magnesium ion binding
E	0008927	molecular_function	mannonate dehydratase activity
E	0009063	biological_process	amino acid catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
E	0047929	molecular_function	gluconate dehydratase activity
F	0000287	molecular_function	magnesium ion binding
F	0008927	molecular_function	mannonate dehydratase activity
F	0009063	biological_process	amino acid catabolic process
F	0016052	biological_process	carbohydrate catabolic process
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding
F	0047929	molecular_function	gluconate dehydratase activity
G	0000287	molecular_function	magnesium ion binding
G	0008927	molecular_function	mannonate dehydratase activity
G	0009063	biological_process	amino acid catabolic process
G	0016052	biological_process	carbohydrate catabolic process
G	0016829	molecular_function	lyase activity
G	0046872	molecular_function	metal ion binding
G	0047929	molecular_function	gluconate dehydratase activity
H	0000287	molecular_function	magnesium ion binding
H	0008927	molecular_function	mannonate dehydratase activity
H	0009063	biological_process	amino acid catabolic process
H	0016052	biological_process	carbohydrate catabolic process
H	0016829	molecular_function	lyase activity
H	0046872	molecular_function	metal ion binding
H	0047929	molecular_function	gluconate dehydratase activity

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKaagmPLyqLLG

Chain	Residue	Details
A	ALA87-GLY112

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250

Chain	Residue	Details
A	TYR161
E	HIS215
F	TYR161
F	HIS215
G	TYR161
G	HIS215
H	TYR161
H	HIS215
A	HIS215
B	TYR161
B	HIS215
C	TYR161
C	HIS215
D	TYR161
D	HIS215
E	TYR161

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING:

Chain	Residue	Details
A	ASN39
B	HIS315
B	ASP319
B	GLU342
C	ASN39
C	GLU265
C	ARG286
C	HIS315
C	ASP319
C	GLU342
D	ASN39
A	GLU265
D	GLU265
D	ARG286
D	HIS315
D	ASP319
D	GLU342
E	ASN39
E	GLU265
E	ARG286
E	HIS315
E	ASP319
A	ARG286
E	GLU342
F	ASN39
F	GLU265
F	ARG286
F	HIS315
F	ASP319
F	GLU342
G	ASN39
G	GLU265
G	ARG286
A	HIS315
G	HIS315
G	ASP319
G	GLU342
H	ASN39
H	GLU265
H	ARG286
H	HIS315
H	ASP319
H	GLU342
A	ASP319
A	GLU342
B	ASN39
B	GLU265
B	ARG286

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS124
B	HIS124
C	HIS124
D	HIS124
E	HIS124
F	HIS124
G	HIS124
H	HIS124

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|Ref.2

Chain	Residue	Details
A	ASP213
E	GLU239
F	ASP213
F	GLU239
G	ASP213
G	GLU239
H	ASP213
H	GLU239
A	GLU239
B	ASP213
B	GLU239
C	ASP213
C	GLU239
D	ASP213
D	GLU239
E	ASP213

site_id	SWS_FT_FI5
Number of Residues	8
Details	SITE: Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity

Chain	Residue	Details
A	PRO317
B	PRO317
C	PRO317
D	PRO317
E	PRO317
F	PRO317
G	PRO317
H	PRO317

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