Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6LRT

Crystal structure of isocitrate lyase (Caur_3889) from Chloroflexus aurantiacus in complex with isocitrate and manganese ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0016829molecular_functionlyase activity
D0019752biological_processcarboxylic acid metabolic process
D0046872molecular_functionmetal ion binding
G0003824molecular_functioncatalytic activity
G0004451molecular_functionisocitrate lyase activity
G0016829molecular_functionlyase activity
G0019752biological_processcarboxylic acid metabolic process
G0046872molecular_functionmetal ion binding
J0003824molecular_functioncatalytic activity
J0004451molecular_functionisocitrate lyase activity
J0016829molecular_functionlyase activity
J0019752biological_processcarboxylic acid metabolic process
J0046872molecular_functionmetal ion binding
M0003824molecular_functioncatalytic activity
M0004451molecular_functionisocitrate lyase activity
M0016829molecular_functionlyase activity
M0019752biological_processcarboxylic acid metabolic process
M0046872molecular_functionmetal ion binding
P0003824molecular_functioncatalytic activity
P0004451molecular_functionisocitrate lyase activity
P0016829molecular_functionlyase activity
P0019752biological_processcarboxylic acid metabolic process
P0046872molecular_functionmetal ion binding
S0003824molecular_functioncatalytic activity
S0004451molecular_functionisocitrate lyase activity
S0016829molecular_functionlyase activity
S0019752biological_processcarboxylic acid metabolic process
S0046872molecular_functionmetal ion binding
V0003824molecular_functioncatalytic activity
V0004451molecular_functionisocitrate lyase activity
V0016829molecular_functionlyase activity
V0019752biological_processcarboxylic acid metabolic process
V0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue ICT A 501
ChainResidue
ATYR85
AARG223
AGLU280
AASN308
ASER310
ASER312
ATHR342
ALEU343
AMN503
ASER87
AGLY88
ATRP89
AASP104
AASP148
ACYS186
AGLY187
AHIS188

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 502
ChainResidue
AARG125
AGLN129
GARG35
GGLN39
GILE40

site_idAC3
Number of Residues3
Detailsbinding site for residue MN A 503
ChainResidue
AASP148
ALYS184
AICT501

site_idAC4
Number of Residues16
Detailsbinding site for residue ICT D 501
ChainResidue
DTYR85
DSER87
DGLY88
DTRP89
DASP148
DCYS186
DGLY187
DHIS188
DARG223
DGLU280
DASN308
DSER310
DSER312
DTHR342
DLEU343
DMN503

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL D 502
ChainResidue
DSER182
DGLU183
GGLY154
GALA181

site_idAC6
Number of Residues4
Detailsbinding site for residue MN D 503
ChainResidue
DTRP89
DASP104
DASP148
DICT501

site_idAC7
Number of Residues16
Detailsbinding site for residue ICT G 501
ChainResidue
GTYR85
GSER87
GGLY88
GTRP89
GASP148
GCYS186
GGLY187
GHIS188
GARG223
GGLU280
GASN308
GSER310
GSER312
GTHR342
GLEU343
GMN504

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL G 502
ChainResidue
DASN158
GALA98
GLEU107
GPRO109

site_idAC9
Number of Residues4
Detailsbinding site for residue GOL G 503
ChainResidue
GSER13
GTRP14
GASP212
GPRO217

site_idAD1
Number of Residues4
Detailsbinding site for residue MN G 504
ChainResidue
GASP104
GASP148
GLYS184
GICT501

site_idAD2
Number of Residues16
Detailsbinding site for residue ICT J 501
ChainResidue
JTYR85
JSER87
JGLY88
JTRP89
JASP148
JCYS186
JGLY187
JHIS188
JARG223
JGLU280
JASN308
JSER310
JSER312
JTHR342
JLEU343
JMN504

site_idAD3
Number of Residues7
Detailsbinding site for residue GOL J 502
ChainResidue
JGLU391
GMET101
JLYS78
JILE130
JTYR131
JTRP141
JARG390

site_idAD4
Number of Residues1
Detailsbinding site for residue GOL J 503
ChainResidue
JGLN402

site_idAD5
Number of Residues4
Detailsbinding site for residue MN J 504
ChainResidue
JASP104
JASP148
JLYS184
JICT501

site_idAD6
Number of Residues15
Detailsbinding site for residue ICT M 501
ChainResidue
MTYR85
MSER87
MGLY88
MTRP89
MASP148
MCYS186
MGLY187
MHIS188
MARG223
MGLU280
MASN308
MSER310
MSER312
MTHR342
MMN502

site_idAD7
Number of Residues4
Detailsbinding site for residue MN M 502
ChainResidue
MASP104
MASP148
MLYS184
MICT501

site_idAD8
Number of Residues16
Detailsbinding site for residue ICT P 501
ChainResidue
PTYR85
PSER87
PGLY88
PTRP89
PASP148
PCYS186
PGLY187
PHIS188
PARG223
PGLU280
PASN308
PSER310
PSER312
PTHR342
PLEU343
PMN503

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL P 502
ChainResidue
PARG35
PVAL38
PILE40
PVAL213
VARG125
VGLN129

site_idAE1
Number of Residues5
Detailsbinding site for residue MN P 503
ChainResidue
PGLY88
PTRP89
PASP104
PASP148
PICT501

site_idAE2
Number of Residues16
Detailsbinding site for residue ICT S 501
ChainResidue
STYR85
SSER87
STRP89
SASP104
SASP148
SCYS186
SGLY187
SHIS188
SARG223
STRP278
SGLU280
SASN308
SSER310
SSER312
STHR342
SMN505

site_idAE3
Number of Residues2
Detailsbinding site for residue GOL S 502
ChainResidue
PASN158
SLEU107

site_idAE4
Number of Residues4
Detailsbinding site for residue GOL S 503
ChainResidue
SSER13
STRP14
SASP212
SPRO217

site_idAE5
Number of Residues5
Detailsbinding site for residue GOL S 504
ChainResidue
MARG125
MGLN129
SARG35
SGLN39
SILE40

site_idAE6
Number of Residues4
Detailsbinding site for residue MN S 505
ChainResidue
SASP148
SLYS184
SARG223
SICT501

site_idAE7
Number of Residues16
Detailsbinding site for residue ICT V 501
ChainResidue
VTYR85
VSER87
VGLY88
VTRP89
VASP148
VCYS186
VGLY187
VHIS188
VARG223
VGLU280
VASN308
VSER310
VSER312
VTHR342
VLEU343
VMN504

site_idAE8
Number of Residues3
Detailsbinding site for residue GOL V 502
ChainResidue
MGLU161
VTYR102
VLEU107

site_idAE9
Number of Residues3
Detailsbinding site for residue GOL V 503
ChainResidue
VGLU50
VTRP53
VASN54

site_idAF1
Number of Residues4
Detailsbinding site for residue MN V 504
ChainResidue
VASP104
VASP148
VLYS184
VICT501

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM
ChainResidueDetails
ALYS184-MET189

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon