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1IHO

CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004592molecular_functionpantoate-beta-alanine ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009058biological_processbiosynthetic process
A0015940biological_processpantothenate biosynthetic process
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0003824molecular_functioncatalytic activity
B0004592molecular_functionpantoate-beta-alanine ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009058biological_processbiosynthetic process
B0015940biological_processpantothenate biosynthetic process
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TRS A 701
ChainResidue
ASER187
AASN190
AARG198

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
AMET30
AGLN61
AILE133
AGLN155
AHOH709

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 703
ChainResidue
BGLN61
BILE133
BGLN155
BHOH741
BHOH825
BMET30

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS37
BHIS37

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AMET30
BGLN155
BMET178
BLEU186
AGLN61
AGLY149
AGLN155
AMET178
ALEU186
BMET30
BGLN61
BGLY149

226707

PDB entries from 2024-10-30

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