Structure of PDB 3pfr Chain D

Receptor sequence
>3pfrD (length=426) Species: 67854 (Actinobacillus succinogenes) [Search protein sequence]
SVPVITDMKVIPVAGHDSMLMNVGGAHSPYFTRNIVILTDNSGHTGVGEA
PGGATIENALTEAIPHVVGRPISILNKIVNDMHNTFELRVNAVAALEAAL
LDLMGQFLGVPVAELLGPGKQRDEVTVLGYLFYVGDDKITDLPYQQPVTG
KHEWYDIRRKKAMDTQAVIELAAASKDRYGFKDFKLKGGVFEGSKEIDTV
IELKKHFPDARITLDPNGCWSLDEAIQLCKGLNDVLTYAEDPCIGENGYS
GREIMAEFRRRTGIPTATNMIATNWREMCHAIMLQSVDIPLADPHFWTLT
GASRVAQLCNEWGLTWGCHSNNHFDISLAMFSHVGAAAPGNPTALDTHWI
WQEGDFYLTKNPLEIKDGKIKLNDKPGLGIELNMDNVLKAHELHKKLPNG
ARNDAIPMQFYYPGWKFDRKRPAMVR
3D structure
PDB3pfr Crystal structure of D-Glucarate dehydratase related protein from Actinobacillus Succinogenes complexed with D-Glucarate
ChainD
Resolution1.899 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K206 K208 D236 N238 E261 N290 D314 H340 N342
Catalytic site (residue number reindexed from 1) K185 K187 D215 N217 E240 N269 D293 H319 N321
Enzyme Commision number ?
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 MG D D236 E261 N290 D215 E240 N269
BS02 GKR D N28 H33 Y151 K208 D236 N238 N290 H340 S341 N342 H369 N22 H27 Y130 K187 D215 N217 N269 H319 S320 N321 H348
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3pfr, PDBe:3pfr, PDBj:3pfr
PDBsum3pfr
PubMed
UniProtA6VQF6

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