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

3VPB

ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine biosynthetic process
A0009085biological_processlysine biosynthetic process
A0016874molecular_functionligase activity
A0036211biological_processprotein modification process
A0042802molecular_functionidentical protein binding
A0043774molecular_functioncoenzyme F420-2 alpha-glutamyl ligase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006526biological_processL-arginine biosynthetic process
B0009085biological_processlysine biosynthetic process
B0016874molecular_functionligase activity
B0036211biological_processprotein modification process
B0042802molecular_functionidentical protein binding
B0043774molecular_functioncoenzyme F420-2 alpha-glutamyl ligase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006526biological_processL-arginine biosynthetic process
C0009085biological_processlysine biosynthetic process
C0016874molecular_functionligase activity
C0036211biological_processprotein modification process
C0042802molecular_functionidentical protein binding
C0043774molecular_functioncoenzyme F420-2 alpha-glutamyl ligase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006526biological_processL-arginine biosynthetic process
D0009085biological_processlysine biosynthetic process
D0016874molecular_functionligase activity
D0036211biological_processprotein modification process
D0042802molecular_functionidentical protein binding
D0043774molecular_functioncoenzyme F420-2 alpha-glutamyl ligase activity
D0046872molecular_functionmetal ion binding
E0006526biological_processL-arginine biosynthetic process
E0009085biological_processlysine biosynthetic process
E0019878biological_processlysine biosynthetic process via aminoadipic acid
E0046872molecular_functionmetal ion binding
F0006526biological_processL-arginine biosynthetic process
F0009085biological_processlysine biosynthetic process
F0019878biological_processlysine biosynthetic process via aminoadipic acid
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 500
ChainResidue
ALYS87
ATYR169
AILE170
AASP176
AARG200
AALA201
AASN202
AASP237
ALEU239
AASN249
AGLU250
ALYS127
AMG502
AZN503
ASO4504
AHOH621
AHOH624
AHOH642
AHOH696
AGLY131
ASER132
ATRP133
AGLY134
AVAL137
AGLN167
AGLU168

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU A 501
ChainResidue
ATYR190
AARG192
AASN202
AVAL203
AALA204
AGLU256
ALYS258
AGLY259
APHE260
ASO4504
AHOH626
AHOH635
EGLU56

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASP237
AGLU250
AADP500
AZN503
ASO4504
AHOH642

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AGLU250
AASN252
AADP500
AMG502
ASO4504
AHOH696

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ASER132
ATRP133
AARG178
AARG192
AASN202
AASP237
AGLU250
AASN252
AADP500
AGLU501
AMG502
AZN503
AHOH642
EGLU56

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP B 500
ChainResidue
BLYS87
BLYS127
BGLY131
BSER132
BTRP133
BGLY134
BGLN167
BGLU168
BTYR169
BILE170
BASP176
BARG200
BALA201
BASN202
BASP237
BASN249
BGLU250
BMG502
BZN503
BSO4504
BHOH617
BHOH621
BHOH650
BHOH651

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GLU B 501
ChainResidue
BSO4504
BHOH654
BHOH658
BHOH689
FGLU56
BARG178
BTYR190
BARG192
BASN202
BVAL203
BALA204
BGLU256
BLYS258
BGLY259
BPHE260

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BASP237
BGLU250
BADP500
BZN503
BSO4504
BHOH650

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BGLU250
BASN252
BADP500
BMG502
BSO4504
BHOH651

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BSER132
BTRP133
BARG178
BARG192
BASN202
BASP237
BGLU250
BASN252
BADP500
BGLU501
BMG502
BZN503
BHOH650
FGLU56

site_idBC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ADP C 500
ChainResidue
CLYS87
CILE125
CLYS127
CGLY131
CSER132
CTRP133
CGLY134
CARG135
CVAL137
CGLN167
CGLU168
CTYR169
CILE170
CASP176
CARG200
CALA201
CASN202
CASP237
CASN249
CGLU250
CMG502
CSO4503
CHOH633
CHOH651
CHOH706
CHOH709
CHOH731

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU C 501
ChainResidue
CTRP133
CTYR190
CARG192
CASN202
CVAL203
CALA204
CGLU256
CLYS258
CGLY259
CPHE260
CSO4503
CHOH639

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 502
ChainResidue
CASP237
CGLU250
CADP500
CSO4503
CHOH709

site_idBC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SO4 C 503
ChainResidue
CSER132
CTRP133
CARG178
CARG192
CASN202
CASP237
CGLU250
CASN252
CADP500
CGLU501
CMG502
CHOH601
CHOH633
CHOH709

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 504
ChainResidue
CSER56
CMET57
CTYR58
DSER159

site_idBC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP D 500
ChainResidue
DLYS87
DILE125
DLYS127
DGLY131
DSER132
DTRP133
DGLY134
DVAL137
DGLN167
DGLU168
DTYR169
DILE170
DASP176
DARG200
DALA201
DASN202
DASP237
DASN249
DGLU250
DMG502
DSO4503
DHOH648
DHOH654
DHOH690
DHOH699

site_idBC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU D 501
ChainResidue
DTRP133
DTYR190
DARG192
DASN202
DVAL203
DALA204
DGLU256
DLYS258
DGLY259
DPHE260
DSO4503
DHOH627
DHOH680

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 502
ChainResidue
DASP237
DGLU250
DADP500
DSO4503
DHOH690

site_idCC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
DSER132
DTRP133
DARG178
DARG192
DASN202
DASP237
DGLU250
DASN252
DADP500
DGLU501
DMG502
DHOH608
DHOH654
DHOH690

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 504
ChainResidue
CSER159
DSER56
DMET57
DTYR58
DHOH803

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 100
ChainResidue
ECYS6
ECYS9
EHIS27
ECYS29

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 100
ChainResidue
FCYS6
FCYS9
FHIS27
FCYS29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsZN_FING: TFIIB-type
ChainResidueDetails
EMET1-GLU34
BLYS127
BGLY131
BGLN167
BARG192
BASN202
BVAL203
BGLU256
CLYS87
CLYS127
CGLY131
FMET1-GLU34
CGLN167
CARG192
CASN202
CVAL203
CGLU256
DLYS87
DLYS127
DGLY131
DGLN167
DARG192
AGLY131
DASN202
DVAL203
DGLU256
AGLN167
AARG192
AASN202
AVAL203
AGLU256
BLYS87

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ECYS6
DASP237
DGLU250
DASN252
ECYS9
EHIS27
ECYS29
FCYS6
FCYS9
FHIS27
FCYS29
CASN252

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 5-glutamyl N2-ornithine; alternate => ECO:0000305
ChainResidueDetails
EGLU56
FGLU56

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon