Structure of PDB 6xdk Chain B

Receptor sequence
>6xdkB (length=355) Species: 522373 (Stenotrophomonas maltophilia K279a) [Search protein sequence]
RAFNFSAGPATLPESVLRQAQAEMLDWHGSGASIVEMSHRGAEFMSVAAE
AEADLRRLLDIPDDYAVLFLSGGATTQQALIPLNFAAPGQRADYVVSGHW
GKTAVKQAGVYVDVNIAASSEANGYRELPARADWQLSRDAAYVHITANET
IHGVEFRDVPDTGNVPLIADFSSSIASEPLDVRRYGVIYAGAQKNLGPVG
VAVMIIRRDLLERSGQPRADIFDYRSHVARNTPPTWNWYLAGLVFKWMLA
EGGVTEFAKRNAAKAALVYGAIDGSGGFYRNEVAYAARSRMNIPFFLPDA
ELDARFVAEAKAAGLLALKGHKVVGGIRASLYNAMPLAGAEALVAFMADF
QQRHG
3D structure
PDB6xdk Crystal structure of Phosphoserine aminotransferase (SerC) from Stenotrophomonas maltophilia K279a
ChainB
Resolution1.6 Å
3D
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
Enzyme Commision number 2.6.1.52: phosphoserine transaminase.
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 CA B G111 V114 D115 G109 V112 D113
BS02 PLP B A76 T77 W102 T152 D172 S174 K196 A74 T75 W100 T150 D170 S172 K194
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6xdk, PDBe:6xdk, PDBj:6xdk
PDBsum6xdk
PubMed
UniProtB2FKF0|SERC_STRMK Phosphoserine aminotransferase (Gene Name=serC)

[Back to BioLiP]