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2CJ9

Crystal structure of Methanosarcina barkeri seryl-tRNA synthetase complexed with an analog of seryladenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004828molecular_functionserine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006434biological_processseryl-tRNA aminoacylation
A0008270molecular_functionzinc ion binding
A0016260biological_processselenocysteine biosynthetic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004828molecular_functionserine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006434biological_processseryl-tRNA aminoacylation
B0008270molecular_functionzinc ion binding
B0016260biological_processselenocysteine biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1503
ChainResidue
ACYS306
AGLU355
ACYS461
ASSA1505

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1504
ChainResidue
ATRP245
ATYR303
AALA304
AGLN305

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1503
ChainResidue
BGLU355
BCYS461
BSSA1505
BCYS306

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B1504
ChainResidue
BVAL240
BTRP245
BTYR303
BALA304
BGLN305

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SSA A1505
ChainResidue
AALA304
AARG336
AGLU338
AVAL348
APHE351
AARG353
AGLU355
ATRP396
AGLN400
AGLU432
APHE433
AGLN434
AASN435
AGLY463
AGLY465
AARG468
AZN1503
AHOH2112
AHOH2149

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SSA B1505
ChainResidue
BALA304
BARG336
BGLU338
BVAL348
BPHE351
BARG353
BGLU355
BTRP396
BGLN400
BGLU432
BPHE433
BGLN434
BASN435
BGLY463
BGLY465
BARG468
BZN1503
BHOH2132
BHOH2151
BHOH2181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBINDING:
ChainResidueDetails
AALA304
AGLU432
AASN435
ACYS461
AARG468
BALA304
BCYS306
BARG336
BGLU338
BARG347
BARG353
ACYS306
BGLU355
BGLN400
BASP416
BGLU432
BASN435
BCYS461
BARG468
AARG336
AGLU338
AARG347
AARG353
AGLU355
AGLN400
AASP416

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
AARG336

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qf6
ChainResidueDetails
BARG336

site_idMCSA1
Number of Residues10
DetailsM-CSA 885
ChainResidueDetails
ACYS306metal ligand
AARG468electrostatic stabiliser
AARG336electrostatic stabiliser
AGLU338metal ligand
AARG347electrostatic stabiliser
AGLU355metal ligand
AASP416metal ligand
AGLU432metal ligand
AASN435metal ligand
ACYS461metal ligand

site_idMCSA2
Number of Residues10
DetailsM-CSA 885
ChainResidueDetails
BCYS306metal ligand
BARG468electrostatic stabiliser
BARG336electrostatic stabiliser
BGLU338metal ligand
BARG347electrostatic stabiliser
BGLU355metal ligand
BASP416metal ligand
BGLU432metal ligand
BASN435metal ligand
BCYS461metal ligand

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PDB entries from 2024-08-28

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