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6EDW

Crystal structure of Mycobacterium tuberculosis ICL2 in the apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004451molecular_functionisocitrate lyase activity
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004451molecular_functionisocitrate lyase activity
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0016829molecular_functionlyase activity
C0019752biological_processcarboxylic acid metabolic process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0016829molecular_functionlyase activity
D0019752biological_processcarboxylic acid metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 801
ChainResidue
AASP17
APHE18
ATHR52
AHOH1026
AHOH1041
AHOH1199
BHIS151

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 802
ChainResidue
BGLY51
BTHR52
BHOH1067
BHOH1098
BHOH1140
AHIS151
BPHE18

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 803
ChainResidue
AALA450
AALA453
AGLN482
AHOH1452
AHOH1477

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 804
ChainResidue
AASP123
AASP177
AASP179
ALYS213
AHOH945
AHOH984

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 801
ChainResidue
BALA450
BALA453
BGLN482
BHOH1560
BHOH1595

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL C 801
ChainResidue
CARG78
CALA472
CHIS476
CLYS513
CMET514
CHOH1107

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL C 802
ChainResidue
CHIS151
CHOH983
CHOH1028
CHOH1092
CHOH1144
DPHE18
DTHR52
DHOH937

site_idAC8
Number of Residues5
Detailsbinding site for residue MG C 803
ChainResidue
CALA450
CALA453
CGLN482
CHOH1454
CHOH1460

site_idAC9
Number of Residues5
Detailsbinding site for residue MG C 804
ChainResidue
CASP177
CASP179
CLYS213
CHOH920
CHOH1217

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL D 801
ChainResidue
CASP17
CPHE18
CTHR52
CHOH955
DHIS151
DHOH1081
DHOH1090
DHOH1151

site_idAD2
Number of Residues5
Detailsbinding site for residue MG D 802
ChainResidue
DALA450
DALA453
DGLN482
DHOH1510
DHOH1524

site_idAD3
Number of Residues6
Detailsbinding site for residue MG D 803
ChainResidue
DASP123
DASP177
DASP179
DLYS213
DHOH922
DHOH934

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHQ
ChainResidueDetails
ALYS213-GLN218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKK7
ChainResidueDetails
ACSX215
BCSX215
CCSX215
DCSX215

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WKK7
ChainResidueDetails
AGLY106
BARG252
BASN487
BTHR522
CGLY106
CASP177
CGLY216
CARG252
CASN487
CTHR522
DGLY106
AASP177
DASP177
DGLY216
DARG252
DASN487
DTHR522
AGLY216
AARG252
AASN487
ATHR522
BGLY106
BASP177
BGLY216

226707

PDB entries from 2024-10-30

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