Structure of PDB 6xdk Chain B Binding Site BS01
Receptor Information
>6xdk Chain B (length=355) Species:
522373
(Stenotrophomonas maltophilia K279a) [
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RAFNFSAGPATLPESVLRQAQAEMLDWHGSGASIVEMSHRGAEFMSVAAE
AEADLRRLLDIPDDYAVLFLSGGATTQQALIPLNFAAPGQRADYVVSGHW
GKTAVKQAGVYVDVNIAASSEANGYRELPARADWQLSRDAAYVHITANET
IHGVEFRDVPDTGNVPLIADFSSSIASEPLDVRRYGVIYAGAQKNLGPVG
VAVMIIRRDLLERSGQPRADIFDYRSHVARNTPPTWNWYLAGLVFKWMLA
EGGVTEFAKRNAAKAALVYGAIDGSGGFYRNEVAYAARSRMNIPFFLPDA
ELDARFVAEAKAAGLLALKGHKVVGGIRASLYNAMPLAGAEALVAFMADF
QQRHG
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
6xdk Chain B Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
6xdk
Crystal structure of Phosphoserine aminotransferase (SerC) from Stenotrophomonas maltophilia K279a
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
G111 V114 D115
Binding residue
(residue number reindexed from 1)
G109 V112 D113
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.6.1.52
: phosphoserine transaminase.
Gene Ontology
Molecular Function
GO:0004648
O-phospho-L-serine:2-oxoglutarate aminotransferase activity
GO:0008483
transaminase activity
GO:0030170
pyridoxal phosphate binding
Biological Process
GO:0006563
L-serine metabolic process
GO:0006564
L-serine biosynthetic process
GO:0008615
pyridoxine biosynthetic process
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6xdk
,
PDBe:6xdk
,
PDBj:6xdk
PDBsum
6xdk
PubMed
UniProt
B2FKF0
|SERC_STRMK Phosphoserine aminotransferase (Gene Name=serC)
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