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1G5Q

EPID H67N COMPLEXED WITH SUBSTRATE PEPTIDE DSYTC

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
A0010181molecular_functionFMN binding
A0015937biological_processcoenzyme A biosynthetic process
A0016829molecular_functionlyase activity
A0071513cellular_componentphosphopantothenoylcysteine decarboxylase complex
D0003824molecular_functioncatalytic activity
D0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
D0010181molecular_functionFMN binding
D0015937biological_processcoenzyme A biosynthetic process
D0016829molecular_functionlyase activity
D0071513cellular_componentphosphopantothenoylcysteine decarboxylase complex
G0003824molecular_functioncatalytic activity
G0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
G0010181molecular_functionFMN binding
G0015937biological_processcoenzyme A biosynthetic process
G0016829molecular_functionlyase activity
G0071513cellular_componentphosphopantothenoylcysteine decarboxylase complex
L0003824molecular_functioncatalytic activity
L0004633molecular_functionphosphopantothenoylcysteine decarboxylase activity
L0010181molecular_functionFMN binding
L0015937biological_processcoenzyme A biosynthetic process
L0016829molecular_functionlyase activity
L0071513cellular_componentphosphopantothenoylcysteine decarboxylase complex
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN A 300
ChainResidue
ATHR10
AASN85
ATHR86
ACYS95
AASP96
ATHR101
AASN115
AMET116
AHOH404
AHOH412
AHOH416
AALA11
AHOH417
AHOH418
AHOH420
DLEU51
MCYS405
ASER12
AILE13
ASER37
APHE43
ALEU65
ASER83
AALA84

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FMN D 301
ChainResidue
ALEU51
DTHR10
DALA11
DSER12
DILE13
DSER37
DPHE43
DSER83
DALA84
DASN85
DTHR86
DASN115
DMET116
DHOH304
DHOH306
DHOH308
DHOH312
DHOH313
DHOH329
DHOH332
LLEU64
LLEU65
LCYS95
LASP96
LTHR101
NCYS405

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FMN G 302
ChainResidue
DLEU64
DLEU65
DCYS95
DASP96
DTHR101
DHOH335
GTHR10
GALA11
GSER12
GILE13
GSER37
GPHE43
GSER83
GALA84
GASN85
GTHR86
GASN115
GMET116
GHOH402
GHOH405
GHOH406
GHOH407
GHOH420
LLEU51
OCYS405

site_idAC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FMN L 303
ChainResidue
LHOH317
LHOH321
PCYS405
GLEU51
GPRO63
GLEU64
GLEU65
GCYS95
GASP96
GTHR101
LTHR10
LALA11
LSER12
LILE13
LSER37
LPHE43
LSER83
LALA84
LASN85
LTHR86
LASN115
LMET116
LHOH304
LHOH305
LHOH310
LHOH315
LHOH316

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS G 401
ChainResidue
DLYS89
DASP96
DHOH333
GLYS89
GASP96
GHOH415
LLYS89
LASP96
LHOH320

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 402
ChainResidue
ALYS89
AASP96
AASP96
AASP96
AHOH405
AHOH426
AHOH426
AHOH426

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsCROSSLNK: S-(2-aminovinyl)-D-cysteine (Ser-Cys) => ECO:0000269|PubMed:3769923
ChainResidueDetails
MSER402
MCYS405
NSER402
NCYS405
OSER402
OCYS405
PSER402
PCYS405

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PDB entries from 2024-05-01

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