Structure of PDB 6ct6 Chain B

Receptor sequence
>6ct6B (length=331) Species: 5804 (Eimeria maxima) [Search protein sequence]
AVFEQNKRPKIALVGSGMIGGTMAFLCSLKELGDVVLFDVVPNMPMGKAM
DLCHNSSVVDNGITVYGSNSYECLTNADVVIITAGITKIPGKWSRMDLLP
VNIKIMREVGGAIKKYCPNAFIINITNPLDVMVAAVQEAANVPKHMICGM
AGMLDSSRLRRMIADCLHVSPHDVQGMVIGVHGDNMLPLMRYITINGIPI
QEFINKGLINKEDINNIYNKTKQAGGDIVRLLGQGSAYYAPGTSAILMAE
SYLKDKKRLFVSSCYLNGQYNVNNHYLGVPCIIGGKGIEQIIELDLNQEE
KKLLQGSIDEVLEMQKAIAALDAGKLEHHHH
3D structure
PDB6ct6 The Mechanistic, Structural, and Evolutionary Origin of Lactate Dehydrogenase Substrate Specificity in Apicomplexa
ChainB
Resolution1.705 Å
3D
structure
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Enzymatic activity
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 NAI B G18 M19 I20 F39 D40 V41 T84 A85 G86 T88 I130 T131 N132 M155 L159 H187 G17 M18 I19 F38 D39 V40 T83 A84 G85 T87 I125 T126 N127 M150 L154 H182
BS02 GLC B N220 Y223 E304 N215 Y218 E299
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6ct6, PDBe:6ct6, PDBj:6ct6
PDBsum6ct6
PubMed
UniProtU6M598

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