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4FIQ

Crystal structure of pyridoxal biosynthesis lyase PdxS from Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A0042819biological_processvitamin B6 biosynthetic process
A0042823biological_processpyridoxal phosphate biosynthetic process
B0016829molecular_functionlyase activity
B0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
B0042819biological_processvitamin B6 biosynthetic process
B0042823biological_processpyridoxal phosphate biosynthetic process
C0016829molecular_functionlyase activity
C0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
C0042819biological_processvitamin B6 biosynthetic process
C0042823biological_processpyridoxal phosphate biosynthetic process
D0016829molecular_functionlyase activity
D0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
D0042819biological_processvitamin B6 biosynthetic process
D0042823biological_processpyridoxal phosphate biosynthetic process
E0016829molecular_functionlyase activity
E0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
E0042819biological_processvitamin B6 biosynthetic process
E0042823biological_processpyridoxal phosphate biosynthetic process
F0016829molecular_functionlyase activity
F0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
F0042819biological_processvitamin B6 biosynthetic process
F0042823biological_processpyridoxal phosphate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS01235
Number of Residues19
DetailsPDXS_SNZ_1 PdxS/SNZ family signature. LPVVNFAAGGVATPADAAL
ChainResidueDetails
ALEU248-LEU266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000255|HAMAP-Rule:MF_01824, ECO:0000269|PubMed:23104439
ChainResidueDetails
ALYS87
BLYS87
CLYS87
DLYS87
ELYS87
FLYS87

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01824, ECO:0000269|PubMed:23104439
ChainResidueDetails
AASP30
CGLY159
CGLY257
CGLY278
DASP30
DGLY159
DGLY257
DGLY278
EASP30
EGLY159
EGLY257
AGLY159
EGLY278
FASP30
FGLY159
FGLY257
FGLY278
AGLY257
AGLY278
BASP30
BGLY159
BGLY257
BGLY278
CASP30

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01824
ChainResidueDetails
AARG171
BARG171
CARG171
DARG171
EARG171
FARG171

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PDB entries from 2024-07-31

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