Structure of PDB 6lds Chain A

Receptor sequence
>6ldsA (length=382) Species: 243232 (Methanocaldococcus jannaschii DSM 2661) [Search protein sequence]
RNMQEKGVSEKEILEELKKYRSLDLKYEDGNIFGSMCSNVLPITRKIVDI
FLETNLGDPGLFKGTKLLEEKAVALLGSLLNNKDAYGHIVSGGTEANLMA
LRCIKNIWREKRRKGLSKNEHPKIIVPITAHFSFEKGREMMDLEYIYAPI
KEDYTIDEKFVKDAVEDYDVDGIIGIAGTTELGTIDNIEELSKIAKENNI
YIHVDAAFGGLVIPFLDDKYKKKGVNYKFDFSLGVDSITIDPHAMGHCPI
PSGGILFKDIGYKRYLDVQATILGTRVGFGGACTYAVLRYLGREGQRKIV
NECMENTLYLYKKLKENNFKPVIEPILNIVAIEDEDYKEVCKKLRDRGIY
VSVVKALRIVVMPHIKREHIDNFIEILNSIKR
3D structure
PDB6lds Structural insights into the mechanism of internal aldimine formation and catalytic loop dynamics in an archaeal Group II decarboxylase.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.11: aspartate 1-decarboxylase.
4.1.1.25: tyrosine decarboxylase.
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 0PR A S36 M37 C38 G94 T95 H132 T181 D206 A208 H244 S35 M36 C37 G93 T94 H131 T180 D205 A207 H243
Gene Ontology
Molecular Function
GO:0004068 aspartate 1-decarboxylase activity
GO:0004837 tyrosine decarboxylase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0015937 coenzyme A biosynthetic process
GO:0019752 carboxylic acid metabolic process
GO:2001120 methanofuran biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6lds, PDBe:6lds, PDBj:6lds
PDBsum6lds
PubMed31445086
UniProtQ60358|MFNA_METJA L-tyrosine/L-aspartate decarboxylase (Gene Name=mfnA)

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