Structure of PDB 3l6c Chain A Binding Site BS01

Receptor Information
>3l6c Chain A (length=322) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DAQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQK
TGSFKIRGALNAIRGLIPDTLEGKPKAVVTHSSGNHGQALTYAAKLEGIP
AYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILV
HPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLK
PSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPI
IRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTV
SPEVKNICIVLSGGNVDLTSLS
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain3l6c Chain A Residue 350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3l6c The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
F55 K56 N86 G186 G187 G188 M189 G239 V240 T285 S313 G314
Binding residue
(residue number reindexed from 1)
F54 K55 N85 G185 G186 G187 M188 G238 V239 T284 S312 G313
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) K55 S83 E209 A213 D215 G238 T284 L311 S312
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3l6c, PDBe:3l6c, PDBj:3l6c
PDBsum3l6c
PubMed20106978
UniProtQ76EQ0|SRR_RAT Serine racemase (Gene Name=Srr)

[Back to BioLiP]