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2Y8N

Crystal structure of glycyl radical enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0016829molecular_functionlyase activity
A0043722molecular_function4-hydroxyphenylacetate decarboxylase activity
B0016829molecular_functionlyase activity
B0043722molecular_function4-hydroxyphenylacetate decarboxylase activity
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0016829molecular_functionlyase activity
C0043722molecular_function4-hydroxyphenylacetate decarboxylase activity
D0016829molecular_functionlyase activity
D0043722molecular_function4-hydroxyphenylacetate decarboxylase activity
D0046872molecular_functionmetal ion binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 B 87
ChainResidue
BHIS3
BCYS6
BASN8
BCYS19
BLEU21
BALA35
BCYS36

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SF4 B 88
ChainResidue
BCYS45
BCYS48
BASN50
BPHE51
BCYS62
BALA77
BCYS80
BSER82
BTYR83
ATRP58
AARG61

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 D 87
ChainResidue
DHIS3
DCYS6
DASN8
DCYS19
DLEU21
DALA35
DCYS36

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SF4 D 88
ChainResidue
CTRP58
CARG61
DCYS45
DCYS48
DASN50
DPHE51
DCYS62
DALA77
DCYS80
DSER82
DTYR83

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pg.GAsPTCGTG
ChainResidueDetails
APRO524-GLY534

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:21823587, ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ
ChainResidueDetails
BHIS3
BCYS19
BCYS36
BCYS45
BCYS48
BCYS62
BCYS80
DHIS3
DCYS6
DCYS19
DCYS36
DCYS45
DCYS48
DCYS62
DCYS80
BCYS6

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21823587
ChainResidueDetails
AGLU505
CGLU505

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:21823587, ECO:0007744|PDB:2YAJ
ChainResidueDetails
ASER344
ACYS503
AHIS536
AGLU637
CSER344
CCYS503
CHIS536
CGLU637

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Glycine radical => ECO:0000255|PROSITE-ProRule:PRU00493, ECO:0000305|PubMed:21823587
ChainResidueDetails
AGLY873
CGLY873

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PDB entries from 2024-06-12

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