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4EPM

Crystal Structure of Arabidopsis GH3.12 (PBS3) in Complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006952biological_processdefense response
A0009626biological_processplant-type hypersensitive response
A0009863biological_processsalicylic acid mediated signaling pathway
A0010112biological_processregulation of systemic acquired resistance
A0016046biological_processdetection of fungus
A0016874molecular_functionligase activity
A0018874biological_processbenzoate metabolic process
A0034052biological_processpositive regulation of plant-type hypersensitive response
A0042742biological_processdefense response to bacterium
A0052625molecular_function4-aminobenzoate amino acid synthetase activity
A0052626molecular_functionbenzoate amino acid synthetase activity
A0052627molecular_functionvanillate amino acid synthetase activity
A0052628molecular_function4-hydroxybenzoate amino acid synthetase activity
A0071456biological_processcellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP A 601
ChainResidue
ASER95
ATYR347
AASP398
APHE414
AARG417
ASER96
AVAL299
ATHR301
ATHR324
ATYR325
AGLY326
ASER327
ASER328

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AGLY97
ATHR98
ALYS104
AARG417
AASN430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EPM, ECO:0007744|PDB:4EQ4, ECO:0007744|PDB:4EQL
ChainResidueDetails
ASER95
ATHR301
ATHR324
ASER328
ATYR347
AASP398

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EQ4, ECO:0007744|PDB:4EQL
ChainResidueDetails
ATYR120

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0007744|PDB:4EQ4
ChainResidueDetails
AARG417

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PDB entries from 2024-07-10

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