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2ZR2

Crystal structure of seryl-tRNA synthetase from Pyrococcus horikoshii complexed with ATP

Replaces:  2DQ1
Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004828molecular_functionserine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006434biological_processseryl-tRNA aminoacylation
A0016260biological_processselenocysteine biosynthetic process
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004828molecular_functionserine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006434biological_processseryl-tRNA aminoacylation
B0016260biological_processselenocysteine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP A1001
ChainResidue
AARG283
ASER373
ATHR406
AALA409
ASER411
AARG412
AGLU285
APHE297
AARG298
AVAL299
APHE302
AGLU370
AVAL371
AVAL372

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A2001
ChainResidue
ASER183
AARG184
AALA289
AHIS300

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A2003
ChainResidue
ALYS291
AASP292
ATHR293
AARG298
AARG369

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A2005
ChainResidue
APHE297
AARG298
AARG369
AGLU370
AARG412
AHOH2011

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A2007
ChainResidue
AALA172
AASP173
APHE174
AALA175

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP B1002
ChainResidue
BARG283
BGLU285
BPHE297
BARG298
BVAL299
BPHE302
BGLU370
BVAL371
BVAL372
BTHR406
BALA409
BSER411
BARG412

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B2002
ChainResidue
BSER183
BARG184
BALA289
BHIS300

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B2004
ChainResidue
BLYS291
BASP292
BTHR293
BARG298
BARG369

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B2006
ChainResidue
BPHE297
BARG298
BARG369
BGLU370
BARG412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00176
ChainResidueDetails
ATHR252
BGLU306
BGLU370
BTHR406
AARG283
AVAL299
AGLU306
AGLU370
ATHR406
BTHR252
BARG283
BVAL299

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
AASP292
AARG298
AGLU285
AARG283
ATHR288

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
BASP292
BARG298
BGLU285
BARG283
BTHR288

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
AARG283

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ses
ChainResidueDetails
BARG283

219140

PDB entries from 2024-05-01

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