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3MF1

Crystal structure of class II aaRS homologue (Bll0957) complexed with an analogue of glycyl adenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006418biological_processtRNA aminoacylation for protein translation
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1000
ChainResidue
ACYS131
AGLU176
ACYS279
AG5A1001

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE G5A A 1001
ChainResidue
APHE172
AMET174
AGLU176
ALYS235
AALA250
ACYS251
AMET252
ASER253
AASN255
ACYS279
AALA281
AGLY283
AARG286
AHOH335
AHOH381
AHOH382
AZN1000
AALA129
ACYS131
AARG159
AGLU161
ALEU169

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1000
ChainResidue
BCYS131
BGLU176
BCYS279
BG5A1001

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE G5A B 1001
ChainResidue
BALA129
BARG159
BGLU161
BLEU169
BPHE172
BMET174
BGLU176
BLYS235
BALA250
BCYS251
BMET252
BSER253
BASN255
BCYS279
BALA281
BGLY283
BARG286
BHOH335
BHOH367
BHOH369
BZN1000

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AGLU176
ALYS235
AALA250
ACYS279
AARG286
BCYS131
BARG159
BGLU161
BARG168
BGLU176
BLYS235
BALA250
BCYS279
BARG286
ACYS131
AARG159
AGLU161
AARG168

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PDB entries from 2024-04-17

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