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2YAJ

CRYSTAL STRUCTURE OF GLYCYL RADICAL ENZYME with bound substrate

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
B0051536molecular_functioniron-sulfur cluster 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
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 87
ChainResidue
BHIS3
BCYS6
BASN8
BCYS19
BLEU21
BCYS36

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

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

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 D 88
ChainResidue
CTRP58
CARG61
DCYS45
DCYS48
DASN50
DCYS62
DALA77
DCYS80
DSER82
DTYR83

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 4HP A 1898
ChainResidue
APHE214
AARG223
ASER344
AGLY345
AVAL399
ALEU400
APHE405
AGLY502
ACYS503
AGLU505
AGLY532
AHIS536
APHE537
AGLU637
AILE750

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 4HP C 1898
ChainResidue
CPHE214
CILE219
CARG223
CSER344
CGLY345
CVAL399
CPHE405
CGLY502
CCYS503
CGLU505
CGLY532
CHIS536
CPHE537
CGLU637

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 Residues1470
DetailsDomain: {"description":"PFL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00887","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues238
DetailsDomain: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Cysteine radical intermediate","evidences":[{"source":"PubMed","id":"21823587","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21823587","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21823587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YAJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21823587","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21823587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YAJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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