Structure of PDB 4ggb Chain A

Receptor sequence
>4ggbA (length=348) Species: 176299 (Agrobacterium fabrum str. C58) [Search protein sequence]
MKITAVRTHLLHVLVEIECDDGTVGWGECLGPARPNAAVVQAYSGWLIGQ
DPRQTEKIWAVLYNALRDQGQRGLSLTALSGIDIALWDIKGKHYGASISM
LLGGRWRESVRAYATGDRVSDNASEMAERRAEGFHACKIKIGFGVEEDLR
VIAAVREAIGPDMRLMIDANHGYTVTEAITLGDRAAGFGIDWFEEPVVPE
QLDAYARVRAGQPIPVAGGETWHGRYGMWQALSAGAVDILQPDLCGCGGF
SEIQKIATLATLHGVRIVPHVWGTGVQIAAALQFMAAMTPDPVRVNPIEP
IMEFDRTHNPFRQAVLREPLEAVNGVVTIPDGPGLGIEINRDALTEFR
3D structure
PDB4ggb Purification, crystallization and structural elucidation of D-galactaro-1,4-lactone cycloisomerase from Agrobacterium tumefaciens involved in pectin degradation.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G50 R53 T134 K164 K166 D194 N196 E220 G245 E246 T247 Q267 D269 H296 V297 W298 R320 E329 F330 H334
Catalytic site (residue number reindexed from 1) G31 R34 T115 K138 K140 D168 N170 E194 G219 E220 T221 Q241 D243 H270 V271 W272 R294 E303 F304 H308
Enzyme Commision number 5.5.1.27: D-galactarolactone cycloisomerase.
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)		 Binding affinity
BS01 CA A D194 E220 E246 D168 E194 E220
BS02 CA A E154 E158 E128 E132
BS03 CA A D209 G237 D183 G211
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ggb, PDBe:4ggb, PDBj:4ggb
PDBsum4ggb
PubMed26750482
UniProtA9CEQ8|GCI_AGRFC D-galactarolactone cycloisomerase (Gene Name=gci)

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