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5DN5

Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ

Functional Information from GO Data
ChainGOidnamespacecontents
A0004040molecular_functionamidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0044780biological_processbacterial-type flagellum assembly
B0004040molecular_functionamidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0044780biological_processbacterial-type flagellum assembly
C0004040molecular_functionamidase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0044780biological_processbacterial-type flagellum assembly
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue IOD A 402
ChainResidue
ASER200
ATYR201

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 403
ChainResidue
AVAL250
AALA251
ATHR254

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD B 401
ChainResidue
BTYR224
BGLY227

site_idAC4
Number of Residues1
Detailsbinding site for residue IOD B 402
ChainResidue
BTYR201

site_idAC5
Number of Residues1
Detailsbinding site for residue IOD C 401
ChainResidue
CLYS233

site_idAC6
Number of Residues2
Detailsbinding site for residue IOD C 402
ChainResidue
ATYR224
AGLY227

site_idAC7
Number of Residues2
Detailsbinding site for residue IOD C 403
ChainResidue
CTYR224
CGLY227

site_idAC8
Number of Residues1
Detailsbinding site for residue IOD C 404
ChainResidue
CTYR201

site_idAC9
Number of Residues2
Detailsbinding site for residue CL C 407
ChainResidue
CALA268
CHOH528

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AGLU223
AASP248
BGLU223
BASP248
CGLU223
CASP248

224572

PDB entries from 2024-09-04

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