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3TA0

A. fulgidus GlnK3, MgATP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006808biological_processregulation of nitrogen utilization
C0030234molecular_functionenzyme regulator activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006808biological_processregulation of nitrogen utilization
D0030234molecular_functionenzyme regulator activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006808biological_processregulation of nitrogen utilization
E0030234molecular_functionenzyme regulator activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006808biological_processregulation of nitrogen utilization
F0030234molecular_functionenzyme regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 200
ChainResidue
AVAL7
AGLY89
AARG90
AHOH145
BGLY27
BMET28
BTHR29
BGLU62
BVAL63
BVAL64
BARG103
AGLY35
AARG36
AGLY37
AGLU38
AGLN39
APHE86
AGLY87
AASP88

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP B 200
ChainResidue
BVAL7
BGLY35
BARG36
BGLY37
BGLU38
BPHE86
BGLY87
BASP88
BGLY89
BARG90
BHOH132
CGLY27
CMET28
CTHR29
CGLU62
CVAL63
CVAL64
CLYS101
CARG103

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 200
ChainResidue
AMET28
ATHR29
AGLU62
AVAL63
AVAL64
ALYS101
AARG103
CVAL7
CGLY35
CARG36
CGLY37
CLYS58
CPHE86
CGLY87
CASP88
CGLY89
CARG90

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP D 200
ChainResidue
DVAL7
DGLY35
DARG36
DGLY37
DGLU38
DLYS58
DPHE86
DGLY87
DGLY89
DARG90
EMET28
ETHR29
EGLU62
EVAL64
ELYS101
EARG103

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP E 200
ChainResidue
EVAL7
EGLY35
EARG36
EGLY37
EGLU38
ELYS58
EPHE86
EGLY87
EASP88
EGLY89
EARG90
EHOH137
FGLY27
FMET28
FTHR29
FGLU62
FVAL63
FVAL64
FLYS101
FARG103

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP F 200
ChainResidue
FVAL7
FGLY35
FARG36
FGLY37
FGLU38
FPHE86
FGLY87
FASP88
FGLY89
FARG90
FHOH121
DGLY27
DMET28
DTHR29
DGLU62
DVAL63
DVAL64
DLYS101
DARG103

Functional Information from PROSITE/UniProt
site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgkfGDGRIFVipV
ChainResidueDetails
ATHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:22039461, ECO:0007744|PDB:3TA0, ECO:0007744|PDB:3TA2
ChainResidueDetails
ATHR29
DTHR29
DGLY37
DVAL64
ETHR29
EGLY37
EVAL64
FTHR29
FGLY37
FVAL64
AGLY37
AVAL64
BTHR29
BGLY37
BVAL64
CTHR29
CGLY37
CVAL64

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22039461, ECO:0007744|PDB:3TA2
ChainResidueDetails
ALYS58
EGLY87
FLYS58
FGLY87
AGLY87
BLYS58
BGLY87
CLYS58
CGLY87
DLYS58
DGLY87
ELYS58

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PDB entries from 2024-07-24

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