Structure of PDB 4e1o Chain D

Receptor sequence
>4e1oD (length=478) Species: 9606 (Homo sapiens) [Search protein sequence]
GSMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPE
DPDSWDSIFGDIERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAI
NCLGFTWASSPACTELEMNVMDWLAKMLGLPEHFLHHHPSSQGGGVLQST
VSESTLIALLAARKNKILEMKTSEPDADESSLNARLVAYASDQAHSSVEK
AGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVFVCATLGTTG
VCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSF
TFNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHW
QIPLSRRFRSVKLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFE
IPAKRHLGLVVFRLKGPNSLTENVLKEIAKAGRLFLIPATIQDKLIIRFT
VTSQFTTRDDILRDWNLIRDAATLILSQ
3D structure
PDB4e1o Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase
ChainD
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.22: histidine 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 PVH D L102 F104 Y334 L103 F105 Y335
BS02 PLP D Y81 T149 V150 S151 H194 T248 D273 A275 K305 Y82 T150 V151 S152 H195 T249 D274 A276 K306
BS03 PVH D Y80 Y81 H194 K305 Y81 Y82 H195 K306
Gene Ontology
Molecular Function
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4e1o, PDBe:4e1o, PDBj:4e1o
PDBsum4e1o
PubMed22767596
UniProtP19113|DCHS_HUMAN Histidine decarboxylase (Gene Name=HDC)

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