Structure of PDB 2c54 Chain B

Receptor sequence

>2c54B (length=360) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]

YTYKELEREQYWPSENLKISITGAGGFIASHIARRLKHEGHYVIASDWKK
NEHMTEDMFCDEFHLVDLRVMENCLKVTEGVDHVFNLAADMGGMGFIQSN
HSVIMYNNTMISFNMIEAARINGIKRFFYASSACIYPEFKQLETTNVSLK
ESDAWPAEPQDAYGLERLATEELCKHYNKDFGIECRIGRFHNIYGPFGTW
KGGREKAPAAFCRKAQTSTDRFEMWGDGLQTRSFTFIDECVEGVLRLTKS
DFREPVNIGSDEMVSMNEMAEMVLSFEEKKLPIHHIPGPEGVRGRNSDNN
LIKEKLGWAPNMRLKEGLRITYFWIKEQIEKEKAKGSDVSLYGSSKVVGT
QAPVQLGSLR

3D structure

PDB

2c54 Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site.

Chain

Resolution

1.5 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	S143 A144 C145 Y174 R178 K217
Catalytic site (residue number reindexed from 1)	S132 A133 C134 Y163 R167 K206
Enzyme Commision number	5.1.3.18: GDP-mannose 3,5-epimerase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	GKE	B	G103 G104 M105 S143 C145 Y174 H202 N203 K217 A218 A221 F222 K225 W236 Q241 R243 M277 P300 E301 S356	G92 G93 M94 S132 C134 Y163 H191 N192 K206 A207 A210 F211 K214 W225 Q230 R232 M266 P289 E290 S345
BS02	GKD	B	G103 G104 M105 S143 F201 H202 N203 K217 A218 A221 F222 K225 W236 Q241 R243 M277 P300 E301 S356	G92 G93 M94 S132 F190 H191 N192 K206 A207 A210 F211 K214 W225 Q230 R232 M266 P289 E290 S345
BS03	NAD	B	G37 F38 I39 D58 W59 V77 D78 L79 L98 A100 M102 I122 A141 S142 S143 Y174 R178 F201 N203 I204 K217	G26 F27 I28 D47 W48 V66 D67 L68 L87 A89 M91 I111 A130 S131 S132 Y163 R167 F190 N192 I193 K206

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0016853	isomerase activity
GO:0047918	GDP-mannose 3,5-epimerase activity
GO:0051287	NAD binding

	Biological Process
GO:0019853	L-ascorbic acid biosynthetic process

	Cellular Component
GO:0005829	cytosol
GO:0009536	plastid

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2c54, PDBe:2c54, PDBj:2c54
PDBsum	2c54
PubMed	16366586
UniProt	Q93VR3\|GME_ARATH GDP-mannose 3,5-epimerase (Gene Name=At5g28840)

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