Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4EM4

Crystal Structure of Staphylococcus aureus bound with the covalent inhibitor Pethyl-VS-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003756molecular_functionprotein disulfide isomerase activity
A0016491molecular_functionoxidoreductase activity
A0050451molecular_functionCoA-disulfide reductase (NADPH) activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
B0003756molecular_functionprotein disulfide isomerase activity
B0016491molecular_functionoxidoreductase activity
B0050451molecular_functionCoA-disulfide reductase (NADPH) activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD A 501
ChainResidue
AVAL7
AASN42
ACYS43
AHIS79
AVAL81
ASER112
APRO113
AGLY114
AARG131
ATYR158
AVAL159
AGLY8
AASN242
APHE245
AGLY276
AASP277
APRO293
ALEU294
AALA295
ACA8508
AHOH608
AHOH610
AVAL10
AHOH613
AHOH623
AHOH634
AHOH646
AHOH682
AHOH757
AHOH781
BTYR419
BALA420
BPRO421
AALA11
AGLY12
APHE32
AGLU33
ALYS34
AASP35

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHOH601
AHOH602
AHOH603
AHOH604
AHOH605
AHOH1149

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AGLU54
AHOH695
AHOH821
AHOH1082

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
APRO2

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 506
ChainResidue
ALYS389

site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE CA8 A 508
ChainResidue
AVAL10
AALA11
AALA14
ATHR15
ASER18
AGLN19
AARG22
ASER39
APHE40
AALA41
AASN42
ACYS43
ALYS71
AALA295
AHIS299
AFAD501
AHOH772
AHOH825
AHOH908
AHOH1159
AHOH1160
AHOH1161
BTYR361
BTYR419
BPRO426
BLYS427
BMET432
BTYR435
BHOH1113

site_idAC7
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD B 501
ChainResidue
BARG131
BTYR158
BASN242
BPHE245
BGLY276
BASP277
BPRO293
BLEU294
BALA295
BCA8506
BHOH601
BHOH604
BHOH607
BHOH609
BHOH639
BHOH641
BHOH642
BHOH658
BHOH682
BHOH707
ATYR419
AALA420
APRO421
BVAL7
BGLY8
BVAL10
BALA11
BGLY12
BPHE32
BGLU33
BLYS34
BASP35
BASN42
BCYS43
BHIS79
BVAL81
BSER112
BPRO113
BGLY114

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BHOH647
BHOH910
BHOH1049
BHOH1102
BHOH1103
BHOH1104

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 505
ChainResidue
BHOH1030

site_idBC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE CA8 B 506
ChainResidue
ATYR361
ATYR419
APRO426
ALYS427
AMET432
ATYR435
AHOH998
AHOH1109
AHOH1150
BVAL10
BALA11
BALA14
BTHR15
BSER18
BGLN19
BARG22
BSER39
BPHE40
BALA41
BASN42
BCYS43
BLYS71
BALA295
BHIS299
BFAD501
BHOH813
BHOH980
BHOH1056

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Redox-active => ECO:0000255|HAMAP-Rule:MF_01608
ChainResidueDetails
ACYS43
BCYS43

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01608
ChainResidueDetails
AGLN19
AARG22
ASER39
AASN42
ALYS71
AVAL151
ATHR267
AHIS299
ATYR419
ALYS427
BGLY8
BTHR15
BGLN19
BARG22
BSER39
BASN42
BLYS71
BVAL151
BTHR267
BHIS299
BTYR419
BLYS427
AGLY8
ATHR15

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon