Structure of PDB 1ez4 Chain D

Receptor sequence
>1ez4D (length=318) Species: 1589 (Lactiplantibacillus pentosus) [Search protein sequence]
SMPNHQKVVLVGDGAVGSSYAFAMAQQGIAEEFVIVDVVKDRTKGDALDL
EDAQAFTAPKKIYSGEYSDCKDADLVVITAGAPQKPGESRLDLVNKNLNI
LSSIVKPVVDSGFDGIFLVAANPVDILTYATWKFSGFPKERVIGSGTSLD
SSRLRVALGKQFNVDPRSVDAYIMGEHGDSEFAAYSTATIGTRPVRDVAK
EQGVSDDDLAKLEDGVRNKAYDIINLKGATFYGIGTALMRISKAILRDEN
AVLPVGAYMDGQYGLNDIYIGTPAIIGGTGLKQIIESPLSADELKKMQDS
AATLKKVLNDGLAELENK
3D structure
PDB1ez4 Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
ChainD
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R106 D166 R169 H193
Catalytic site (residue number reindexed from 1) R90 D150 R153 H177
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 NAD D G29 A30 V31 D52 V53 T95 A96 G97 I116 A136 A137 N138 H193 I251 G14 A15 V16 D37 V38 T79 A80 G81 I100 A120 A121 N122 H177 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ez4, PDBe:1ez4, PDBj:1ez4
PDBsum1ez4
PubMed11807949
UniProtP56511|LDH_LACPE L-lactate dehydrogenase (Gene Name=ldh)

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