Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3CIS

The Crystal Structure of Rv2623 from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide binding
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
C0000166molecular_functionnucleotide binding
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
D0000166molecular_functionnucleotide binding
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
E0000166molecular_functionnucleotide binding
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
F0000166molecular_functionnucleotide binding
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
G0000166molecular_functionnucleotide binding
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
H0000166molecular_functionnucleotide binding
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 Residues160
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of universal stress protein Rv2623 from mycobacterium tuberculosis.","authoringGroup":["Mycobacterium tuberculosis structural genomics consortium (TB)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"PDB data bank","title":"The crystal structure of Rv2623: a novel, tandem-repeat universal stress protein of Mycobacterium tuberculosis.","authors":["Drumm J.","Mi K.","Bilder P.","Almo S.","Chan J."]}},{"source":"PDB","id":"2JAX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CIS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon