Structure of PDB 3qm3 Chain D

Receptor sequence
>3qm3D (length=344) Species: 197 (Campylobacter jejuni) [Search protein sequence]
SNAMGVLDIVKAGVISGDELNKIYDYAKAEGFAIPAVNVVGTDSINAVLE
AAKKVNSPVIIQFSNGGAKFYAGKNCPNGEVLGAISGAKHVHLLAKAYGV
PVILHTDHAARKLLPWIDGLIEANAQYKKTHGQALFSSHMLDLSEESLEE
NLSTCEVYLQKLDALGVALEIELGCTGGTGIDNSKLYTQPEDVALAYERL
GKISDKFSIAASFGNVHGVSLQPEILKNSQKFVKDKFALNSDKPINFVFH
GGSGSELKDIKNAVSYGVIKMNIDTDTQWAFWDGVREYELKNRAYLQGQI
GNPEGDDKPNKKYYDPRVWLRSGEESMIKRLEIAFEDLNCINKN
3D structure
PDB3qm3 1.85 Angstrom Resolution Crystal Structure of Fructose-bisphosphate Aldolase (Fba) from Campylobacter jejuni
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D104 H105 H221 H260 N282
Catalytic site (residue number reindexed from 1) D107 H108 H217 H250 N272
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 ZN D H105 E169 H221 H260 H108 E172 H217 H250
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
Cellular Component
GO:0005829 cytosol

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External links
PDB RCSB:3qm3, PDBe:3qm3, PDBj:3qm3
PDBsum3qm3
PubMed
UniProtQ0PAS0|ALF_CAMJE Fructose-bisphosphate aldolase (Gene Name=fba)

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