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3EPL

Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0046872molecular_functionmetal ion binding
A0052381molecular_functiontRNA dimethylallyltransferase activity
B0000049molecular_functiontRNA binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008270molecular_functionzinc ion binding
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0046872molecular_functionmetal ion binding
B0052381molecular_functiontRNA dimethylallyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 6IA E 37
ChainResidue
ATHR23
EA36
EA38
AASP46
AMET48
ATHR112
AARG220
AGLN256
AARG288
ATYR292
AARG295

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS375
ACYS378
AHIS397
AHIS403

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DMA A 422
ChainResidue
ATHR22
ATHR23
AGLY24
AVAL25
AGLY26
ALYS27
ASER28
AASN59
AARG220
AHOH437

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG E 72
ChainResidue
EU55
EC56
EG57

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BCYS375
BCYS378
BHIS397
BHIS403

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2
ChainResidue
BSER28
BASN59
BDMA422

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DMA B 422
ChainResidue
BMG2
BTHR23
BGLY24
BVAL25
BGLY26
BLYS27
BSER28
BASN59
BARG220
BHOH456

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG F 72
ChainResidue
FC2
FHOH100

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG F 73
ChainResidue
FA26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsZN_FING: Matrin-type
ChainResidueDetails
ATYR373-ARG409
BTYR373-ARG409

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY21
BGLY21

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18852462
ChainResidueDetails
ATHR23
BTHR23

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18852462, ECO:0007744|PDB:3EPH, ECO:0007744|PDB:3EPJ, ECO:0007744|PDB:3EPK, ECO:0007744|PDB:3EPL
ChainResidueDetails
AHIS397
AHIS403
BCYS375
BCYS378
BHIS397
BHIS403
ACYS375
ACYS378

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Interaction with substrate tRNA => ECO:0000269|PubMed:18852462
ChainResidueDetails
BTHR112
BGLN193
ATHR112
AGLN193

221051

PDB entries from 2024-06-12

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