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2J9E

Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006808biological_processregulation of nitrogen utilization
C0030234molecular_functionenzyme regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 1116
ChainResidue
AGLU14
AHOH2111
AHOH2112
BGLU79
CILE15
CLYS18

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1117
ChainResidue
ALYS3
BLYS3
CLYS3

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1118
ChainResidue
AARG103
BARG82

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 1119
ChainResidue
BGLU14
BLYS17
CHOH2087

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 1116
ChainResidue
CATP1115
CHOH2052
CHOH2066
CHOH2137

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL C 1117
ChainResidue
AHOH2005
CLYS3
CGLU5
CLYS60
CGLU62
CHOH2010

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 1118
ChainResidue
BARG103
CGLY84

site_idAC8
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ATP A 1115
ChainResidue
AILE7
AGLY35
AARG36
AGLY37
AVAL38
AGLN39
ALYS58
APRO86
AGLY87
AASP88
AGLY89
ALYS90
AHOH2083
AHOH2103
AHOH2104
AHOH2105
AHOH2106
AHOH2107
AHOH2108
AHOH2109
AHOH2110
CGLY27
CMET28
CTHR29
CGLU62
CLEU63
CVAL64
CARG101
CARG103

site_idAC9
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP B 1118
ChainResidue
AGLY27
AMET28
ATHR29
AGLU62
ALEU63
AVAL64
AARG101
AARG103
BILE7
BGLY35
BARG36
BGLY37
BVAL38
BGLN39
BLYS58
BPRO86
BGLY87
BASP88
BGLY89
BLYS90
BHOH2105
BHOH2135
BHOH2136
BHOH2137

site_idBC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP C 1115
ChainResidue
CHOH2052
CHOH2065
CHOH2066
CHOH2137
CHOH2138
CHOH2139
CHOH2140
BGLY27
BMET28
BTHR29
BGLU62
BVAL64
BARG101
BARG103
BHIS115
CILE7
CGLY35
CARG36
CGLY37
CVAL38
CLYS58
CPRO86
CGLY87
CASP88
CGLY89
CLYS90
CMG1116

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AKG C 1119
ChainResidue
CGLU50
CTYR51
CILE52
CVAL53
CASP54
CHOH2141
CHOH2142
CHOH2143

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:17203075, ECO:0007744|PDB:2J9C, ECO:0007744|PDB:2J9E
ChainResidueDetails
ATHR29
BARG101
CTHR29
CVAL38
CVAL64
CPRO86
CARG101
AVAL38
AVAL64
APRO86
AARG101
BTHR29
BVAL38
BVAL64
BPRO86

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17203075
ChainResidueDetails
AILE52
BILE52
CILE52

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17203075, ECO:0007744|PDB:2J9D
ChainResidueDetails
AASP88
BASP88
CASP88

218853

PDB entries from 2024-04-24

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