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2DSO

Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0005737cellular_componentcytoplasm
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
E0005737cellular_componentcytoplasm
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
F0005737cellular_componentcytoplasm
F0016787molecular_functionhydrolase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AGLU48
AASN138
AASN185
AASP236
ASER237
AHOH5034
AHOH5104

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BASN185
BASP236
BSER237
BHOH1011
BHOH1038
BHOH1151
BGLU48
BASN138

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA C 1003
ChainResidue
CGLU48
CASN138
CASN185
CASP236
CSER237
CHOH1037
CHOH1040
CHOH1133

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA D 1004
ChainResidue
DGLU48
DASN138
DASN185
DASP236
DSER237
DHOH5012
DHOH5018
DHOH5084

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA E 1005
ChainResidue
EGLU48
EASN138
EASN185
EASP236
ESER237
EHOH1072
EHOH1175

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA F 1006
ChainResidue
FGLU48
FASN138
FASN185
FASP236
FSER237
FHOH1047
FHOH1139

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
ASER110
AGLY112
AASP130
ATHR133
ATYR135

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1008
ChainResidue
BSER110
BGLY112
BASP130
BTHR133
BTYR135

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA C 1009
ChainResidue
CSER110
CTHR111
CGLY112
CASP130
CTHR133
CALA134
CTYR135
CHOH1120

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 1010
ChainResidue
DSER110
DGLY112
DASP130
DTHR133
DTYR135

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 1011
ChainResidue
ESER110
EGLY112
EASP130
ETHR133
ETYR135

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 1012
ChainResidue
FSER110
FGLY112
FASP130
FTHR133
FTYR135

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 5001
ChainResidue
DCYS239
DILE240
DGLN286
DPHE287
DGLY318
DHIS319
DHOH5016
DHOH5108

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 5002
ChainResidue
ALYS16
AHOH5097
BSER27
BHOH1093

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 5003
ChainResidue
DLYS16
DILE23
FSER27
FTHR31
FHOH1098

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AASP236
BASP236
CASP236
DASP236
EASP236
FASP236

site_idSWS_FT_FI2
Number of Residues60
DetailsBINDING:
ChainResidueDetails
DGLU48
DSER110
DGLY112
DASP130
DTHR133
DTYR135
DASN138
DASN185
DASP236
DSER237
EGLU48
ESER110
EGLY112
EASP130
ETHR133
ETYR135
EASN138
EASN185
EASP236
ESER237
FGLU48
FSER110
FGLY112
FASP130
FTHR133
FTYR135
FASN138
FASN185
FASP236
FSER237
AGLU48
ASER110
AGLY112
AASP130
ATHR133
ATYR135
AASN138
AASN185
AASP236
ASER237
BGLU48
BSER110
BGLY112
BASP130
BTHR133
BTYR135
BASN138
BASN185
BASP236
BSER237
CGLU48
CSER110
CGLY112
CASP130
CTHR133
CTYR135
CASN138
CASN185
CASP236
CSER237

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PDB entries from 2024-05-29

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