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3CIS

The Crystal Structure of Rv2623 from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009274cellular_componentpeptidoglycan-based cell wall
A0040008biological_processregulation of growth
A0085014biological_processdormancy entry of symbiont in host
B0001666biological_processresponse to hypoxia
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009274cellular_componentpeptidoglycan-based cell wall
B0040008biological_processregulation of growth
B0085014biological_processdormancy entry of symbiont in host
C0001666biological_processresponse to hypoxia
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0009274cellular_componentpeptidoglycan-based cell wall
C0040008biological_processregulation of growth
C0085014biological_processdormancy entry of symbiont in host
D0001666biological_processresponse to hypoxia
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0009274cellular_componentpeptidoglycan-based cell wall
D0040008biological_processregulation of growth
D0085014biological_processdormancy entry of symbiont in host
E0001666biological_processresponse to hypoxia
E0005524molecular_functionATP binding
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0009274cellular_componentpeptidoglycan-based cell wall
E0040008biological_processregulation of growth
E0085014biological_processdormancy entry of symbiont in host
F0001666biological_processresponse to hypoxia
F0005524molecular_functionATP binding
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0009274cellular_componentpeptidoglycan-based cell wall
F0040008biological_processregulation of growth
F0085014biological_processdormancy entry of symbiont in host
G0001666biological_processresponse to hypoxia
G0005524molecular_functionATP binding
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0009274cellular_componentpeptidoglycan-based cell wall
G0040008biological_processregulation of growth
G0085014biological_processdormancy entry of symbiont in host
H0001666biological_processresponse to hypoxia
H0005524molecular_functionATP binding
H0005829cellular_componentcytosol
H0005886cellular_componentplasma membrane
H0009274cellular_componentpeptidoglycan-based cell wall
H0040008biological_processregulation of growth
H0085014biological_processdormancy entry of symbiont in host
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
AASP198

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG C 1002
ChainResidue
CASP198

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 2002
ChainResidue
DASP198

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG E 1002
ChainResidue
EASP198

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG F 2002
ChainResidue
FASP198

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG G 1002
ChainResidue
GASP198

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 1101
ChainResidue
ASER17
AALA20
AALA43
AGLY117
ALEU119
AGLY120
ASER121
AGLY122
AARG123
AARG127
AGLY130
ASER131
ASER133
AGLY13
AILE14
AASP15

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 1102
ChainResidue
AGLY165
AASP167
ASER172
ALEU193
AALA195
AASP198
APRO245
AGLY262
AARG264
AGLY265
AARG266
AGLY267
AGLY268
AMET272
AGLY275
ASER276
AGLY278

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B 2101
ChainResidue
BGLY13
BILE14
BASP15
BSER17
BALA20
BALA43
BALA100
BLEU104
BGLY117
BLEU119
BGLY120
BSER121
BGLY122
BARG123
BARG127
BGLY130
BSER131
BSER133

site_idBC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 2102
ChainResidue
BGLY165
BASP167
BSER172
BLEU193
BALA195
BASP198
BPRO245
BGLY262
BARG264
BGLY265
BARG266
BGLY267
BGLY268
BMET272
BGLY275
BSER276
BGLY278

site_idBC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP C 1101
ChainResidue
CGLY13
CILE14
CASP15
CSER17
CALA20
CALA43
CGLY117
CLEU119
CGLY120
CSER121
CGLY122
CARG123
CARG127
CGLY130
CSER131
CSER133

site_idBC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 1102
ChainResidue
CARG264
CGLY265
CGLY267
CGLY268
CMET272
CGLY275
CSER276
CGLY278
CGLY165
CASP167
CSER172
CLEU193
CHIS194
CALA195
CASP198
CPRO245
CGLY262

site_idBC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP D 2101
ChainResidue
DGLY13
DILE14
DASP15
DSER17
DALA20
DALA43
DALA100
DLEU104
DGLY117
DLEU119
DGLY120
DSER121
DGLY122
DARG123
DARG127
DGLY130
DSER131
DSER133

site_idBC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP D 2102
ChainResidue
DGLY165
DASP167
DLEU193
DALA195
DASP198
DPRO245
DGLY262
DARG264
DGLY265
DARG266
DGLY267
DGLY268
DMET272
DGLY275
DSER276
DGLY278

site_idBC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP E 1101
ChainResidue
EGLY13
EILE14
EASP15
ESER17
EALA20
EALA43
EGLY117
ELEU119
EGLY120
ESER121
EGLY122
EARG123
EARG127
EGLY130
ESER131
ESER133

site_idBC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP E 1102
ChainResidue
EGLY165
EASP167
ESER172
ELEU193
EALA195
EASP198
EPRO245
EGLY262
EARG264
EGLY265
EGLY267
EGLY268
EMET272
EGLY275
ESER276
EGLY278

site_idCC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP F 2101
ChainResidue
FGLY13
FILE14
FASP15
FSER17
FALA43
FGLY117
FLEU119
FGLY120
FSER121
FGLY122
FARG123
FARG127
FGLY130
FSER131
FSER133

site_idCC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP F 2102
ChainResidue
FGLY165
FASP167
FLEU193
FALA195
FASP198
FPRO245
FGLY262
FARG264
FGLY265
FARG266
FGLY267
FGLY268
FMET272
FGLY275
FSER276
FGLY278

site_idCC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP G 1101
ChainResidue
GGLY13
GILE14
GASP15
GSER17
GALA20
GALA43
GGLY117
GLEU119
GGLY120
GSER121
GGLY122
GARG123
GARG127
GGLY130
GSER131
GSER133

site_idCC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP G 1102
ChainResidue
GGLY165
GASP167
GSER172
GLEU193
GHIS194
GALA195
GASP198
GPRO245
GGLY262
GARG264
GGLY265
GARG266
GGLY267
GGLY268
GMET272
GGLY275
GSER276
GGLY278

site_idCC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP H 2101
ChainResidue
HGLY13
HILE14
HASP15
HSER17
HALA20
HALA43
HALA100
HGLY117
HLEU119
HGLY120
HSER121
HGLY122
HARG123
HARG127
HGLY130
HSER131
HSER133

site_idCC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP H 2102
ChainResidue
HGLY165
HASP167
HSER172
HLEU193
HALA195
HASP198
HPRO245
HGLY262
HARG264
HGLY265
HARG266
HGLY267
HGLY268
HMET272
HGLY275
HSER276
HGLY278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsBINDING: BINDING => ECO:0000269|Ref.11, ECO:0000269|Ref.12, ECO:0007744|PDB:2JAX, ECO:0007744|PDB:3CIS
ChainResidueDetails
AGLY13
BGLY13
BALA43
BGLY117
BARG127
BSER131
BGLY165
BASP198
BGLY262
BSER276
CGLY13
AALA43
CALA43
CGLY117
CARG127
CSER131
CGLY165
CASP198
CGLY262
CSER276
DGLY13
DALA43
AGLY117
DGLY117
DARG127
DSER131
DGLY165
DASP198
DGLY262
DSER276
EGLY13
EALA43
EGLY117
AARG127
EARG127
ESER131
EGLY165
EASP198
EGLY262
ESER276
FGLY13
FALA43
FGLY117
FARG127
ASER131
FSER131
FGLY165
FASP198
FGLY262
FSER276
GGLY13
GALA43
GGLY117
GARG127
GSER131
AGLY165
GGLY165
GASP198
GGLY262
GSER276
HGLY13
HALA43
HGLY117
HARG127
HSER131
HGLY165
AASP198
HASP198
HGLY262
HSER276
AGLY262
ASER276

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PDB entries from 2024-09-11

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