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4H2V

Crystal structure of Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with glycylated carrier protein

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
C0000035molecular_functionacyl binding
C0000036molecular_functionacyl carrier activity
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006633biological_processfatty acid biosynthetic process
C0009245biological_processlipid A biosynthetic process
D0000035molecular_functionacyl binding
D0000036molecular_functionacyl carrier activity
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0006633biological_processfatty acid biosynthetic process
D0009245biological_processlipid A biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS131
AGLU176
ACYS279
CH2V101

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 402
ChainResidue
AALA250
ACYS251
AMET252
ASER253
AALA281
AGLY283
AARG286
AHOH512
AHOH529
AHOH531
AHOH592
AHOH616
CH2V101
AARG159
AGLU161
ALEU169
APHE172
ALYS235

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 403
ChainResidue
AARG58
AHOH580

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 404
ChainResidue
ASER56
AHIS57
AARG58
BASP184
BASP185

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 405
ChainResidue
AHIS29
ASER30
AHOH611

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS131
BGLU176
BCYS279
BHOH645

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AMP B 402
ChainResidue
BARG159
BGLU161
BLEU169
BPHE172
BMET174
BLYS235
BALA250
BCYS251
BMET252
BSER253
BGLY283
BARG286
BHOH501
BHOH528
BHOH540

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
AHOH547
AHOH548
BSER118
BHOH506
BHOH507
BHOH559

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 404
ChainResidue
BSER163
BHIS165
BARG168
BHOH628

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 405
ChainResidue
BARG168
BARG286
BHOH540
BHOH600
BHOH604

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 406
ChainResidue
AHOH552
BHIS29
BSER30
BHOH598

site_idBC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE H2V C 101
ChainResidue
AALA129
ACYS131
ATYR132
AGLU176
APHE217
ALYS225
AGLN229
AASN255
AHIS257
ACYS279
AZN401
AAMP402
CTHR41
CSER42

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PNS D 1000
ChainResidue
BTYR132
BASP215
BGLN229
BGLN232
BASN255
BHIS257
BHOH587
BHOH622
BHOH646
DTHR41
DSER42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258
ChainResidueDetails
AGLU176
ALYS235
AALA250
ACYS279
AARG286
BCYS131
BARG159
BGLU161
BARG168
BGLU176
BLYS235
BALA250
BCYS279
BARG286
AGLU161
AARG168
CSER42
DSER42

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PDB entries from 2024-04-17

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