1AJZ

STRUCTURE OF DIHYDROPTEROATE PYROPHOSPHORYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004156	molecular_function	dihydropteroate synthase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009396	biological_process	folic acid-containing compound biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016740	molecular_function	transferase activity
A	0042558	biological_process	pteridine-containing compound metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 283

Chain	Residue
A	ASN22
A	ARG63
A	ARG255
A	HIS257
A	HOH320
A	HOH323
A	HOH360

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 284

Chain	Residue
A	HOH290
A	HOH313
A	SER222
A	ARG235

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Functional Information from PROSITE/UniProt

site_id	PS00792
Number of Residues	16
Details	DHPS_1 Dihydropteroate synthase signature 1. VmGILNvTpDSFsDgG

Chain	Residue	Details
A	VAL17-GLY32

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site_id	PS00793
Number of Residues	14
Details	DHPS_2 Dihydropteroate synthase signature 2. GAtIIDVGGesTrP

Chain	Residue	Details
A	GLY51-PRO64

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P9WND1

Chain	Residue	Details
A	ASN22

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:9187658, ECO:0007744|PDB:1AJ2

Chain	Residue	Details
A	THR62
A	ASP96
A	ASN115
A	ASP185
A	LYS221
A	ARG255

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1aj0

Chain	Residue	Details
A	ASN22
A	ARG255
A	ARG63

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 394

Chain	Residue	Details
A	LYS221	activator
A	ARG255	activator

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