Structure of PDB 4plc Chain B

Receptor sequence

>4plcB (length=324) Species: 5794 (Apicomplexa)

MTKRKKISLIGSGMIGGTMAYLCAQKELGDVVLFDVVKNMPQGKALDLSH
SSSIADTNVKVTGTNSYEDIKGSDVVIITAGLTKAPGKSDKEWSRDDLLP
FNAKIMREVGENIKKYCPNAFVIVITNPLDVMVKVLHEHSGLPKNKVCGM
AGVLDSSRFRHFIAEKLNVSPRDVQAMVIGAHGDKMVPLTRYVTVNGIPL
QEFIKKGRITQEEIDEIVERTKNAGGEIVNLLGQGSAYFAPAASAIEMAE
AYLKDKKRVLVCSCYLEGQYGHKDMFVGVPAVIGGNGVEKVIELELTPEE
KELFDKSVEEVRKLQKAIKALGLE

3D structure

• PDB: 4plc An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
• Chain: B
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R99 D159 R162 H186
• Catalytic site (residue number reindexed from 1): R95 D155 R158 H182
• 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	PYR	B	W97 R99 R162 H186	W93 R95 R158 H182
BS02	NAD	B	G17 M18 I19 F38 D39 V40 T83 A84 G85 L86 T87 I109 I129 N131 M154 H186 P245	G13 M14 I15 F34 D35 V36 T79 A80 G81 L82 T83 I105 I125 N127 M150 H182 P241

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• 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:0019752 carboxylic acid metabolic process

External links

• PDB: RCSB:4plc, PDBe:4plc, PDBj:4plc
• PDBsum: 4plc
• PubMed: 24966208
• UniProt: A0A075B5G8