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4Q2T

Crystal structure of Arginyl-tRNA synthetase complexed with L-arginine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004814molecular_functionarginine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006420biological_processarginyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004814molecular_functionarginine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006420biological_processarginyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ARG A 601
ChainResidue
AASP125
APHE344
AGOL602
AHOH703
ASER128
AASN130
AHIS139
AHIS165
ATYR312
AASP316
ATYR334
AGLN340

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
ASER127
AHIS136
ASER142
AVAL336
AASP337
APHE369
AARG601

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ARG B 601
ChainResidue
BASP125
BSER128
BASN130
BHIS139
BHIS165
BTYR312
BASP316
BTYR334
BVAL336
BGLN340
BPHE344
BGOL602
BHOH705

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 602
ChainResidue
BSER127
BHIS136
BSER142
BVAL336
BASP337
BARG601

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKeMHVGHL
ChainResidueDetails
APRO129-LEU140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24859084, ECO:0007744|PDB:4Q2T
ChainResidueDetails
APHE200
BLYS412
AGLU211
ASER384
AVAL388
ALYS412
BPHE200
BGLU211
BSER384
BVAL388

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

223166

PDB entries from 2024-07-31

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