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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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P9WKK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WKK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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