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3ED1

Crystal Structure of Rice GID1 complexed with GA3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0009739biological_processresponse to gibberellin
A0009740biological_processgibberellic acid mediated signaling pathway
A0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
A0010325biological_processraffinose family oligosaccharide biosynthetic process
A0010331molecular_functiongibberellin binding
A0016787molecular_functionhydrolase activity
A0048444biological_processfloral organ morphogenesis
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0009739biological_processresponse to gibberellin
B0009740biological_processgibberellic acid mediated signaling pathway
B0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
B0010325biological_processraffinose family oligosaccharide biosynthetic process
B0010331molecular_functiongibberellin binding
B0016787molecular_functionhydrolase activity
B0048444biological_processfloral organ morphogenesis
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0009739biological_processresponse to gibberellin
C0009740biological_processgibberellic acid mediated signaling pathway
C0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
C0010325biological_processraffinose family oligosaccharide biosynthetic process
C0010331molecular_functiongibberellin binding
C0016787molecular_functionhydrolase activity
C0048444biological_processfloral organ morphogenesis
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0009739biological_processresponse to gibberellin
D0009740biological_processgibberellic acid mediated signaling pathway
D0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
D0010325biological_processraffinose family oligosaccharide biosynthetic process
D0010331molecular_functiongibberellin binding
D0016787molecular_functionhydrolase activity
D0048444biological_processfloral organ morphogenesis
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0009739biological_processresponse to gibberellin
E0009740biological_processgibberellic acid mediated signaling pathway
E0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
E0010325biological_processraffinose family oligosaccharide biosynthetic process
E0010331molecular_functiongibberellin binding
E0016787molecular_functionhydrolase activity
E0048444biological_processfloral organ morphogenesis
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0009739biological_processresponse to gibberellin
F0009740biological_processgibberellic acid mediated signaling pathway
F0009939biological_processpositive regulation of gibberellic acid mediated signaling pathway
F0010325biological_processraffinose family oligosaccharide biosynthetic process
F0010331molecular_functiongibberellin binding
F0016787molecular_functionhydrolase activity
F0048444biological_processfloral organ morphogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 501
ChainResidue
ALEU23
ALEU49
AASP50
AARG51
AHOH629

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 A 601
ChainResidue
AARG35
AGLN249
ATRP253
AHOH827

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GA3 A 401
ChainResidue
APHE27
AARG35
AGLY122
ASER123
AILE133
ATYR134
AASP197
ASER198
AVAL246
AASP250
AARG251
ATYR254
AVAL326
AGLY327
ATYR329
AHOH623
AHOH645

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 602
ChainResidue
ATHR231
AASP264
AARG265

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NO3 A 603
ChainResidue
ALEU331

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 604
ChainResidue
AASN26
ASER30
BHIS19
BLEU23
BARG51
BPO4701

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 501
ChainResidue
BLEU23
BASN26
BSER30
BLEU49
BASP50
BARG51
BHOH712

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 B 601
ChainResidue
BARG35
BTRP253
BHOH871

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 B 602
ChainResidue
BTHR231
BASP264
BARG265

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 701
ChainResidue
BARG51
BLEU330
BLEU331
BNO3604
BHOH760

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GA3 B 401
ChainResidue
BILE24
BPHE27
BARG35
BGLY122
BSER123
BILE133
BTYR134
BASP197
BSER198
BVAL246
BASP250
BARG251
BTYR254
BVAL326
BGLY327
BTYR329
BHOH702
BHOH740

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD C 501
ChainResidue
CASN26
CSER30
CLEU49
CASP50
CARG51
CHOH699
DARG51

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 C 602
ChainResidue
CTHR231
CASP264
CARG265
CHOH756

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 C 604
ChainResidue
CASN26
CSER30
DHIS19
DLEU23
DARG51

site_idBC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GA3 C 401
ChainResidue
CARG251
CTYR254
CVAL326
CGLY327
CTYR329
CHOH615
CHOH621
CHOH701
CILE24
CPHE27
CARG35
CGLY122
CSER123
CILE133
CTYR134
CASP197
CSER198
CVAL246
CASP250

site_idBC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GA3 D 401
ChainResidue
DPHE27
DARG35
DGLY122
DSER123
DILE133
DTYR134
DASP197
DSER198
DVAL246
DASP250
DARG251
DTYR254
DVAL326
DGLY327
DTYR329
DHOH618
DHOH628
DHOH658
DHOH781

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD D 501
ChainResidue
DASN26
DLEU49
DASP50
DARG51
DHOH697

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NO3 D 603
ChainResidue
DLEU330
DLEU331

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 D 601
ChainResidue
DARG35
DGLN249
DHOH708

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 E 701
ChainResidue
EARG51
ETHR132
ESER136
ELEU330
EHOH746

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD E 501
ChainResidue
EASN26
ESER30
ELEU49
EARG51
EHOH714
FARG51
FMPD501

site_idCC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GA3 E 401
ChainResidue
EPHE27
EARG35
EGLY122
ESER123
EILE133
ETYR134
EASP197
ESER198
EVAL246
EASP250
EARG251
ETYR254
EVAL326
EGLY327
ETYR329
EHOH717
EHOH720

site_idCC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GA3 F 401
ChainResidue
FPHE27
FARG35
FGLY122
FSER123
FILE133
FTYR134
FASP197
FSER198
FVAL246
FASP250
FARG251
FTYR254
FVAL326
FGLY327
FTYR329
FHOH619
FHOH661

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD F 501
ChainResidue
EMPD501
FLEU23
FSER30
FLEU49
FARG51
FHOH640

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 F 602
ChainResidue
FTHR231
FASP264
FARG265

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 F 603
ChainResidue
FSER136
FLEU330
FLEU331
FHOH615

Functional Information from PROSITE/UniProt
site_idPS01173
Number of Residues17
DetailsLIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. IIfFHGGSFvhsSasST
ChainResidueDetails
AILE116-THR132

site_idPS01174
Number of Residues13
DetailsLIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. VfLSGDSSGGnIA
ChainResidueDetails
AVAL192-ALA204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsMotif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10038","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19037316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19037316","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ED1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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