Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KPL

Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with Mg,d-mannonate and 2-keto-3-deoxy-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 PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CS2 A 501

Chain	Residue
A	ASN39
A	PRO317
A	ASP319
A	GLU342
A	TRP405
A	MG503
A	HOH618
E	TYR77
E	TRP78
A	HIS124
A	ARG149
A	ASP213
A	HIS215
A	GLU239
A	GLU265
A	ARG286
A	HIS315

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 502

Chain	Residue
A	PRO82
A	VAL83
E	PRO82
E	VAL83
E	THR84

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 503

Chain	Residue
A	ASP213
A	GLU239
A	GLU265
A	CS2501
A	HOH829

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CS2 B 501

Chain	Residue
B	ASN39
B	HIS124
B	ARG149
B	ASP213
B	HIS215
B	GLU239
B	GLU265
B	ARG286
B	HIS315
B	PRO317
B	ASP319
B	GLU342
B	LEU392
B	TRP405
B	MG502
B	HOH620
D	TYR77
D	TRP78

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	ASP213
B	GLU239
B	GLU265
B	CS2501
B	HOH838

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE KDG C 501

Chain	Residue
C	ASN39
C	HIS124
C	ASP213
C	HIS215
C	GLU239
C	GLU265
C	ARG286
C	HIS315
C	PRO317
C	ASP319
C	GLU342
C	TRP405
C	MG503
C	HOH602
G	TYR77
G	TRP78

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 502

Chain	Residue
C	PRO82
C	VAL83
G	PRO82
G	VAL83

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 503

Chain	Residue
C	ASP213
C	GLU239
C	GLU265
C	ARG286
C	KDG501
C	HOH824

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE KDG D 501

Chain	Residue
B	TRP78
D	ASN39
D	HIS124
D	ARG149
D	ASP213
D	HIS215
D	GLU239
D	GLU265
D	ARG286
D	HIS315
D	PRO317
D	ASP319
D	GLU342
D	TRP405
D	MG503
D	HOH621

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 502

Chain	Residue
B	PRO82
B	VAL83
D	GLY81
D	PRO82
D	VAL83

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 503

Chain	Residue
D	GLU265
D	KDG501
D	HOH820
D	ASP213
D	GLU239

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CS2 E 501

Chain	Residue
A	TRP78
E	ASN39
E	HIS124
E	ARG149
E	ASP213
E	HIS215
E	GLU239
E	GLU265
E	ARG286
E	HIS315
E	PRO317
E	ASP319
E	GLU342
E	TRP405
E	MG502
E	HOH606
E	HOH837

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 502

Chain	Residue
E	ASP213
E	GLU239
E	GLU265
E	CS2501
E	HOH849

site_id	BC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CS2 F 501

Chain	Residue
F	ASN39
F	HIS124
F	ASP213
F	HIS215
F	GLU239
F	GLU265
F	ARG286
F	HIS315
F	PRO317
F	ASP319
F	GLU342
F	TRP405
F	MG503
F	HOH621
H	TYR77
H	TRP78

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 502

Chain	Residue
F	PRO82
F	VAL83
H	GLY81
H	PRO82
H	VAL83

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 503

Chain	Residue
F	ASP213
F	GLU239
F	GLU265
F	CS2501
F	HOH839

site_id	BC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE KDG G 501

Chain	Residue
C	TRP78
G	ASN39
G	HIS124
G	ARG149
G	ASP213
G	HIS215
G	GLU239
G	GLU265
G	ARG286
G	HIS315
G	PRO317
G	ASP319
G	GLU342
G	TRP405
G	MG503
G	HOH602

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL G 502

Chain	Residue
C	GLU245
G	TRP69
G	TYR73
G	SER269
G	HIS271
G	HOH775
G	HOH779

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 503

Chain	Residue
G	ASP213
G	GLU239
G	GLU265
G	KDG501
G	HOH846

site_id	CC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE KDG H 501

Chain	Residue
F	TYR77
F	TRP78
H	ASN39
H	HIS124
H	ARG149
H	ASP213
H	HIS215
H	GLU239
H	GLU265
H	ARG286
H	HIS315
H	PRO317
H	ASP319
H	GLU342
H	TRP405
H	MG502
H	HOH630

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG H 502

Chain	Residue
H	ASP213
H	GLU239
H	GLU265
H	KDG501
H	HOH843

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	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant P317A of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate.","authors":["Fedorov A.A.","Fedorov E.V.","Wichelecki D.","Gerlt J.A.","Almo S.C."]}}]}

Chain

Residue

Details

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

Chain

Residue

Details

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