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4TS1

CRYSTAL STRUCTURE OF A DELETION MUTANT OF A TYROSYL-T/RNA SYNTHETASE COMPLEXED WITH TYROSINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004831molecular_functiontyrosine-tRNA ligase activity
B0005524molecular_functionATP binding
B0006418biological_processtRNA aminoacylation for protein translation
B0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYR A 320
ChainResidue
ATYR34
AGLN195
AHOH348
AHOH375
AGLY36
AASP38
ALEU68
AASP78
ATYR169
AGLN173
AASP176
AGLN189

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYR B 320
ChainResidue
BTYR34
BGLY36
BASP38
BASP78
BTYR169
BGLN173
BASP176
BGLN189
BGLN195
BHOH351
BHOH389

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHIGHL
ChainResidueDetails
APRO39-LEU49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1TYD
ChainResidueDetails
ATYR34
ATYR169
BTYR34
BTYR169

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250, ECO:0007744|PDB:1TYD
ChainResidueDetails
AGLN173
AASP176
BGLN173
BASP176

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS233
BLYS233

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS233
ALYS230

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS233
BLYS230

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
AARG86
ALYS82
ALYS233
ALYS230

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BARG86
BLYS82
BLYS233
BLYS230

site_idMCSA1
Number of Residues10
DetailsM-CSA 197
ChainResidueDetails
ATHR40electrostatic stabiliser, hydrogen bond donor
ATHR234electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand
AHIS45electrostatic stabiliser, hydrogen bond donor
AHIS48electrostatic stabiliser, hydrogen bond donor
ALYS82electrostatic stabiliser, hydrogen bond donor
AARG86electrostatic stabiliser, hydrogen bond donor
AGLN173electrostatic stabiliser, hydrogen bond acceptor
AASP194electrostatic stabiliser, hydrogen bond acceptor
ALYS230electrostatic stabiliser, hydrogen bond donor
ALYS233electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues10
DetailsM-CSA 197
ChainResidueDetails
BTHR40electrostatic stabiliser, hydrogen bond donor
BTHR234electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand
BHIS45electrostatic stabiliser, hydrogen bond donor
BHIS48electrostatic stabiliser, hydrogen bond donor
BLYS82electrostatic stabiliser, hydrogen bond donor
BARG86electrostatic stabiliser, hydrogen bond donor
BGLN173electrostatic stabiliser, hydrogen bond acceptor
BASP194electrostatic stabiliser, hydrogen bond acceptor
BLYS230electrostatic stabiliser, hydrogen bond donor
BLYS233electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-26

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