Structure of PDB 3hmk Chain A Binding Site BS01

Receptor Information
>3hmk Chain A (length=321) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKT
GSFKIRGALNAIRGLIPDTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPA
YIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVH
PNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKP
SVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPII
RDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVS
PEVKNICIVLSGGNVDLTSLS
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3hmk Chain A Residue 340 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3hmk The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		E210 A214 D216
Binding residue
(residue number reindexed from 1)		E208 A212 D214
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K56 S84 E210 A214 D216 G239 T285 L312 S313
Catalytic site (residue number reindexed from 1) K54 S82 E208 A212 D214 G237 T283 L310 S311
Enzyme Commision number 4.3.1.17: L-serine ammonia-lyase.
4.3.1.18: D-serine ammonia-lyase.
5.1.1.18: serine racemase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003941 L-serine ammonia-lyase activity
GO:0005509 calcium ion binding
GO:0005524 ATP binding
GO:0008721 D-serine ammonia-lyase activity
GO:0016594 glycine binding
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0018114 threonine racemase activity
GO:0030165 PDZ domain binding
GO:0030170 pyridoxal phosphate binding
GO:0030378 serine racemase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006563 L-serine metabolic process
GO:0009069 serine family amino acid metabolic process
GO:0009410 response to xenobiotic stimulus
GO:0014070 response to organic cyclic compound
GO:0032496 response to lipopolysaccharide
GO:0042866 pyruvate biosynthetic process
GO:0070178 D-serine metabolic process
GO:0070179 D-serine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0043025 neuronal cell body
GO:0045177 apical part of cell

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hmk, PDBe:3hmk, PDBj:3hmk
PDBsum3hmk
PubMed20106978
UniProtQ76EQ0|SRR_RAT Serine racemase (Gene Name=Srr)

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