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5IE2

Crystal structure of a plant enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006952biological_processdefense response
A0009506cellular_componentplasmodesma
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0010030biological_processpositive regulation of seed germination
A0010214biological_processseed coat development
A0016874molecular_functionligase activity
A0033611biological_processoxalate catabolic process
A0048046cellular_componentapoplast
A0050203molecular_functionoxalate-CoA ligase activity
A0050832biological_processdefense response to fungus
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006952biological_processdefense response
B0009506cellular_componentplasmodesma
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0010030biological_processpositive regulation of seed germination
B0010214biological_processseed coat development
B0016874molecular_functionligase activity
B0033611biological_processoxalate catabolic process
B0048046cellular_componentapoplast
B0050203molecular_functionoxalate-CoA ligase activity
B0050832biological_processdefense response to fungus
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue ATP A 601
ChainResidue
ATHR170
AGLU310
AALA311
AALA313
AMET314
ATHR315
AVAL337
AASP394
ALEU406
AARG409
ALYS500
ASER171
AMG602
AACY603
AHOH731
AHOH742
AHOH756
AHOH758
AHOH814
AHOH816
AHOH892
AGLY172
ATHR173
ATHR174
AHIS214
ASER289
AALA290
ASER291

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 602
ChainResidue
AATP601
AHOH742
AHOH756
AHOH758
AHOH816

site_idAC3
Number of Residues8
Detailsbinding site for residue ACY A 603
ChainResidue
AHIS214
AVAL215
AHIS216
ASER289
AALA313
AMET314
AHIS319
AATP601

site_idAC4
Number of Residues27
Detailsbinding site for residue ATP B 601
ChainResidue
BTHR170
BSER171
BGLY172
BTHR173
BTHR174
BHIS214
BSER289
BALA290
BSER291
BGLU310
BALA311
BALA313
BMET314
BTHR315
BVAL337
BASP394
BLEU406
BARG409
BLYS500
BMG602
BACY603
BHOH727
BHOH728
BHOH798
BHOH819
BHOH874
BHOH887

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 602
ChainResidue
BATP601
BHOH727
BHOH728
BHOH798
BHOH819

site_idAC6
Number of Residues8
Detailsbinding site for residue ACY B 603
ChainResidue
BHIS214
BVAL215
BHIS216
BSER289
BALA313
BMET314
BHIS319
BATP601

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. FLHTSGTTSrPK
ChainResidueDetails
APHE167-LYS178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3
ChainResidueDetails
ATHR170
AGLU310
ATHR315
AASP394
BTHR170
BGLU310
BTHR315
BASP394

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE2
ChainResidueDetails
AHIS214
AARG409
BHIS214
BARG409

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O24146
ChainResidueDetails
AARG239
AGLY418
BARG239
BGLY418

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27326693, ECO:0007744|PDB:5IE3
ChainResidueDetails
ASER289
AMET314
AHIS319
ALYS500
BSER289
BMET314
BHIS319
BLYS500

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1

222624

PDB entries from 2024-07-17

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