Structure of PDB 3l6b Chain A

Receptor sequence
>3l6bA (length=322) Species: 9606 (Homo sapiens) [Search protein sequence]
AQYDISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKT
GSFKIRGALNAVRSLVRKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVP
QTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEP
AVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVY
AAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVD
DIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKN
ICIVLSGGNVDLTSSITWVKQA
3D structure
PDB3l6b The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 S77 E203 A207 D209 G232 T278 L305 S306
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.
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 PLP A F55 K56 N86 G185 G186 G187 G188 M189 V240 E283 T285 S313 G314 F53 K54 N79 G178 G179 G180 G181 M182 V233 E276 T278 S306 G307
BS02 MN A E210 A214 D216 E203 A207 D209
BS03 MLI A K56 S83 S84 N86 H87 R135 G239 K54 S76 S77 N79 H80 R128 G232
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:0005515 protein 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:0005829 cytosol
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:3l6b, PDBe:3l6b, PDBj:3l6b
PDBsum3l6b
PubMed20106978
UniProtQ9GZT4|SRR_HUMAN Serine racemase (Gene Name=SRR)

[Back to BioLiP]