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4FIY

Crystal Structure of GlfT2 Complexed with UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008921molecular_functionlipopolysaccharide-1,6-galactosyltransferase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0035250molecular_functionUDP-galactosyltransferase activity
A0035496molecular_functionlipopolysaccharide-1,5-galactosyltransferase activity
A0044038biological_processcell wall macromolecule biosynthetic process
A0045227biological_processcapsule polysaccharide biosynthetic process
A0046872molecular_functionmetal ion binding
A0052573biological_processUDP-D-galactose metabolic process
A0070592biological_processcell wall polysaccharide biosynthetic process
A0071555biological_processcell wall organization
A0071769biological_processmycolate cell wall layer assembly
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008921molecular_functionlipopolysaccharide-1,6-galactosyltransferase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0035250molecular_functionUDP-galactosyltransferase activity
B0035496molecular_functionlipopolysaccharide-1,5-galactosyltransferase activity
B0044038biological_processcell wall macromolecule biosynthetic process
B0045227biological_processcapsule polysaccharide biosynthetic process
B0046872molecular_functionmetal ion binding
B0052573biological_processUDP-D-galactose metabolic process
B0070592biological_processcell wall polysaccharide biosynthetic process
B0071555biological_processcell wall organization
B0071769biological_processmycolate cell wall layer assembly
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UDP A 701
ChainResidue
APHE169
AHIS396
AMN702
AARG171
AGLN200
AASN229
AGLY231
AGLY232
AASP256
APHE367
AILE368

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 702
ChainResidue
AARG171
AASP256
AASP258
AHIS396
AUDP701

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
ASER31
ATHR32
ATHR33
AASN34

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UDP B 701
ChainResidue
BPHE169
BARG171
BGLN200
BASN229
BGLY231
BGLY232
BPHE367
BLYS369
BHIS396
BASP403
BMN702

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 702
ChainResidue
BARG171
BASP256
BASP258
BHIS396
BUDP701

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22707726
ChainResidueDetails
AASP372
BASP372

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:22707726
ChainResidueDetails
AARG171
AGLN200
AASN229
AASP256
BARG171
BGLN200
BASN229
BASP256

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22707726
ChainResidueDetails
AASP258
AHIS396
BASP258
BHIS396

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PDB entries from 2024-05-01

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