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2IGL

Crystal Structure of E. coli YEDX, a transthyretin related protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0006144biological_processpurine nucleobase metabolic process
A0016787molecular_functionhydrolase activity
A0032991cellular_componentprotein-containing complex
A0033971molecular_functionhydroxyisourate hydrolase activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0051289biological_processprotein homotetramerization
B0006144biological_processpurine nucleobase metabolic process
B0016787molecular_functionhydrolase activity
B0032991cellular_componentprotein-containing complex
B0033971molecular_functionhydroxyisourate hydrolase activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0051289biological_processprotein homotetramerization
C0006144biological_processpurine nucleobase metabolic process
C0016787molecular_functionhydrolase activity
C0032991cellular_componentprotein-containing complex
C0033971molecular_functionhydroxyisourate hydrolase activity
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0051289biological_processprotein homotetramerization
D0006144biological_processpurine nucleobase metabolic process
D0016787molecular_functionhydrolase activity
D0032991cellular_componentprotein-containing complex
D0033971molecular_functionhydroxyisourate hydrolase activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0051289biological_processprotein homotetramerization
Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. HILNqqtGkPAadVtV
ChainResidueDetails
AHIS32-VAL47

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YHVPllLSQYGYS
ChainResidueDetails
ATYR120-SER132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS32
DHIS32
DARG70
DTYR134
AARG70
ATYR134
BHIS32
BARG70
BTYR134
CHIS32
CARG70
CTYR134

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PDB entries from 2024-07-24

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