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6O5J

Crystal Structure of DAD2 bound to quinazolinone derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0010223biological_processsecondary shoot formation
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A1901601biological_processstrigolactone biosynthetic process
B0010223biological_processsecondary shoot formation
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B1901601biological_processstrigolactone biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue LM7 A 301
ChainResidue
APHE27
APHE194
AHIS218
ASER219
AHIS246
AHOH401
AHOH448
AHOH483
AHOH515
ASER96
APHE125
APHE135
AVAL143
ATRP154
APHE158
APHE174
ASER190

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 302
ChainResidue
ATYR131
AHIS132
ASER223
AVAL224
BASN230

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 303
ChainResidue
AARG36
AASP72
APRO253
ATHR254
AHOH420

site_idAC4
Number of Residues16
Detailsbinding site for residue LM7 B 301
ChainResidue
BPHE27
BSER96
BPHE125
BPHE135
BVAL143
BTRP154
BPHE158
BPHE174
BSER190
BPHE194
BHIS218
BSER219
BHIS246
BHOH425
BHOH473
BHOH493

site_idAC5
Number of Residues3
Detailsbinding site for residue PEG B 302
ChainResidue
BLEU6
BASP7
BVAL11

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL B 303
ChainResidue
AHOH423
BASP130
BHIS132
BSER223
BVAL224
BHOH578

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:22959345
ChainResidueDetails
ASER96
BSER96

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q10QA5
ChainResidueDetails
AASP217
BASP217

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:22959345
ChainResidueDetails
AHIS246
BHIS246

223166

PDB entries from 2024-07-31

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