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3PYB

Crystal structure of ent-copalyl diphosphate synthase from Arabidopsis thaliana in complex with 13-aza-13,14-dihydrocopalyl diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0008299biological_processisoprenoid biosynthetic process
A0009507cellular_componentchloroplast
A0009686biological_processgibberellin biosynthetic process
A0009740biological_processgibberellic acid mediated signaling pathway
A0009905molecular_functionent-copalyl diphosphate synthase activity
A0010333molecular_functionterpene synthase activity
A0016102biological_processditerpenoid biosynthetic process
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0008299biological_processisoprenoid biosynthetic process
B0009507cellular_componentchloroplast
B0009686biological_processgibberellin biosynthetic process
B0009740biological_processgibberellic acid mediated signaling pathway
B0009905molecular_functionent-copalyl diphosphate synthase activity
B0010333molecular_functionterpene synthase activity
B0016102biological_processditerpenoid biosynthetic process
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0008299biological_processisoprenoid biosynthetic process
C0009507cellular_componentchloroplast
C0009686biological_processgibberellin biosynthetic process
C0009740biological_processgibberellic acid mediated signaling pathway
C0009905molecular_functionent-copalyl diphosphate synthase activity
C0010333molecular_functionterpene synthase activity
C0016102biological_processditerpenoid biosynthetic process
C0016829molecular_functionlyase activity
C0016853molecular_functionisomerase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE A3C A 901
ChainResidue
AASP149
AHIS182
ALYS186
AGLU193
AGLN791
ASER795
APHE799
AHOH846

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE A 911
ChainResidue
ALYS444
ATYR448
ATYR483
ATYR427

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE A 921
ChainResidue
ASER657
APHE658
AASP667
AASN669
CSER137
CLYS140

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 1PE A 931
ChainResidue
AASP380
ATYR511

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1PE A 811
ChainResidue
ALYS140
BASN654
BSER657
BPHE658
BPHE661
BASP667
BASN669

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1PE B 911
ChainResidue
BHOH38
BTYR427
BLYS441
BLYS444
BGLU445
BTYR483
BGLU749

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE B 931
ChainResidue
BILE208
BASP377
BTYR511

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE B 921
ChainResidue
BPRO136
BLYS140
CASN654
CSER657
CPHE658
CASP667

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE C 911
ChainResidue
CTYR427
CLYS444
CTYR448
CTYR483
CGLU749
CHOH825

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE C 931
ChainResidue
CILE208
CASP377
CASP379
CASP380
CTYR511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21602811, ECO:0007744|PDB:3PYA
ChainResidueDetails
ALYS245
ALYS463
BLYS245
BLYS463
CLYS245
CLYS463

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:C7BKP9
ChainResidueDetails
AASP377
AASP379
BASP377
BASP379
CASP377
CASP379

219140

PDB entries from 2024-05-01

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