Structure of PDB 1lth Chain T

Receptor sequence

>1lthT (length=313) Species: 1679 (Bifidobacterium longum subsp. longum)

PTKLAVIGAGAVGSTLAFAAAQRGIAREIVLEDIAKERVEAEVLDMQHGS
SFYPTVSIDGSDDPEICRDADMVVITAGPRQKPGQSRLELVGATVNILKA
IMPNLVKVAPNAIYMLITNPVDIATHVAQKLTGLPENQIFGSGTNLDSAR
LRFLIAQQTGVNVKNVHAYIAGEHGDSEVPLWESATIGGVPMSDWTPLPG
HDPLDADKREEIHQEVKNAAYKIINGKGATNYAIGMSGVDIIEAVLHDTN
RILPVSSMLKDFHGISDICMSVPTLLNRQGVNNTINTPVSDKELAALKRS
AETLKETAAQFGF

3D structure

• PDB: 1lth T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
• Chain: T
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H180
• Catalytic site (residue number reindexed from 1): H174
• Enzyme Commision number: 1.1.1.27: L-lactate 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	FBP	T	R158 K170 N171 H173 Y175	R152 K164 N165 H167 Y169
BS02	NAD	T	A17 V18 D39 I40 R44 T82 A83 G84 R86 I103 I107 I123 N125 H180 N237 I240	A11 V12 D33 I34 R38 T76 A77 G78 R80 I97 I101 I117 N119 H174 N231 I234

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004459 L-lactate dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Biological Process

• GO:0006089 lactate metabolic process
• GO:0006090 pyruvate metabolic process
• GO:0006096 glycolytic process
• GO:0019752 carboxylic acid metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1lth, PDBe:1lth, PDBj:1lth
• PDBsum: 1lth
• PubMed: 7656036
• UniProt: E8ME30|LDH2_BIFL2 L-lactate dehydrogenase 2 (Gene Name=ldh2)