Structure of PDB 1lj8 Chain A

Receptor sequence
>1lj8A (length=492) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
MKLNKQNLTQLAPEVKLPAYTLADTRQGIAHIGVGGFHRAHQAYYTDALM
NTGEGLDWSICGVGLRSEDRKARDDLAGQDYLFTLYELGDTDDTEVRVIG
SISDMLLAEDSAQALIDKLASPEIRIVSLTITEGGYCIDDSNGEFMAHLP
QIQHDLAHPSSPKTVFGFICAALTQRRAAGIPAFTVMSCDNLPHNGAVTR
KALLAFAALHNAELHDWIKAHVSFPNAMVDRITPMTSTAHRLQLHDEHGI
DDAWPVVCEPFVQWVLEDKFVNGRPAWEKVGVQFTDDVTPYEEMKIGLLN
GSHLALTYLGFLKGYRFVHETMNDPLFVAYMRAYMDLDVTPNLAPVPGID
LTDYKQTLVDRFSNQAIADQLERVCSDGSSKFPKFTVPTINRLIADGRET
ERAALVVAAWALYLKGVDENGVSYTIPDPRAEFCQGLVSDDALISQRLLA
VEEIFGTAIPNSPEFVAAFERCYGSLRDNGVTTTLKHLLKKP
3D structure
PDB1lj8 Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.67: mannitol 2-dehydrogenase.
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 NAD A G33 V34 G35 G36 F37 R66 D69 I131 T132 E133 D190 N191 R231 I232 T233 R373 G33 V34 G35 G36 F37 R66 D69 I131 T132 E133 D190 N191 R231 I232 T233 R373
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0050086 mannitol 2-dehydrogenase activity
Biological Process
GO:0019594 mannitol metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1lj8, PDBe:1lj8, PDBj:1lj8
PDBsum1lj8
PubMed12196534
UniProtO08355

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