Structure of PDB 6zsp Chain BBB

Receptor sequence
>6zspBBB (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
QYDISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTG
SFKIRGALNAVRSLVPKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQ
TAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPA
VIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYA
AEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDD
IFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNI
CIVLSGGNVDLTSSITWVK
3D structure
PDB6zsp Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase.
ChainBBB
Resolution1.6 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 L312 S313
Catalytic site (residue number reindexed from 1) K53 S76 E202 A206 D208 G231 L304 S305
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 MG BBB E210 A214 D216 E202 A206 D208
BS02 MLI BBB X56 S83 S84 N86 H87 R135 G239 S242 X53 S75 S76 N78 H79 R127 G231 S234
BS03 ATP BBB S31 S32 I33 E276 R277 K279 S28 S29 I30 E268 R269 K271
BS04 ATP BBB H24 K51 T52 G53 Q89 Y121 N316 H21 K48 T49 G50 Q81 Y113 N308
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:6zsp, PDBe:6zsp, PDBj:6zsp
PDBsum6zsp
PubMed35410329
UniProtQ9GZT4|SRR_HUMAN Serine racemase (Gene Name=SRR)

[Back to BioLiP]