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4WF2

Structure of E. coli BirA G142A bound to biotinol-5'-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000976molecular_functiontranscription cis-regulatory region binding
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0004077molecular_functionbiotin--[biotin carboxyl-carrier protein] ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006355biological_processregulation of DNA-templated transcription
A0006768biological_processbiotin metabolic process
A0009102biological_processbiotin biosynthetic process
A0009374molecular_functionbiotin binding
A0016874molecular_functionligase activity
A0017053cellular_componenttranscription repressor complex
A0036211biological_processprotein modification process
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue BTX A 501
ChainResidue
ASER89
ATRP123
APHE124
ASER134
ALYS183
AGLY186
AILE187
AALA205
AGLY206
AASN208
ATRP223
ATHR90
AHOH652
AGLN112
AGLY115
AARG116
AGLY117
AARG118
AARG121
ALYS122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsDNA_BIND: H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00978
ChainResidueDetails
AGLY22-GLN41

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ASER89
AARG116

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00978, ECO:0000269|PubMed:11353844, ECO:0000269|PubMed:1409631
ChainResidueDetails
AGLN112
ALYS183

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 538
ChainResidueDetails
AARG118electrostatic stabiliser
ALYS183electrostatic stabiliser
AARG317

238268

PDB entries from 2025-07-02

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