Structure of PDB 4rlg Chain D

Receptor sequence
>4rlgD (length=470) Species: 479434 (Sphaerobacter thermophilus DSM 20745) [Search protein sequence]
NAMDSRFLPATAFIDPEGRNRNEVERLVQQVVDLILAKLTGAAERPPMPE
ITIPEAAATEATLLQAIRDMVDGSMNPANPGYIGHMDPMPATMAILGDLV
AAAVNNNMLSLEMSPSFSRLETLLLRAIAGLFGLGEQAGGVLTSGGSLAN
LQALAVARNVAFDSVEPGITGLAQRPVIFASEAAHTSLQKAAMLLGLGTA
AVIPVRATADSRMDPEDLRARIDQARGAGQHPFCVVATAGTTTTGNIDPL
AEIGAIAREHGLWFHVDAAYGGALVFSERHRWRLAGIEQADSITFNPQKW
LYVAKTCAMVLFRDAGVLERAFRIPPYMRATDGFINLGEIGVQGTRHADV
VKLWLTLQHIGQQGYARLIDDGYRLAERVVEGVRQRPFLRLAGEIDTNIV
CFRGEPDWLPAERWDDWNAALQALLLREGKIFLSLPVYRGGRWLRAVLLN
PYTTDAVIDAMFKQIDRFAG
3D structure
PDB4rlg The clear crystal structure of pyridoxal-dependent decarboxylase from sphaerobacter thermophilus dsm 20745
ChainD
Resolution1.901 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.15: glutamate 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 PMP D G150 G151 S152 H190 T247 D272 A274 N301 X304 G145 G146 S147 H185 T242 D267 A269 N296 X299
BS02 ABU D S186 A189 H190 T191 S181 A184 H185 T186
BS03 ABU D A189 H190 T191 Q194 A184 H185 T186 Q189
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological 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:4rlg, PDBe:4rlg, PDBj:4rlg
PDBsum4rlg
PubMed
UniProtD1C7D8

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