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3BN1

Crystal structure of GDP-perosamine synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000271biological_processpolysaccharide biosynthetic process
A0008483molecular_functiontransaminase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0102933molecular_functionGDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity
B0000271biological_processpolysaccharide biosynthetic process
B0008483molecular_functiontransaminase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0009243biological_processO antigen biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0102933molecular_functionGDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity
C0000271biological_processpolysaccharide biosynthetic process
C0008483molecular_functiontransaminase activity
C0009103biological_processlipopolysaccharide biosynthetic process
C0009243biological_processO antigen biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
C0102933molecular_functionGDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity
D0000271biological_processpolysaccharide biosynthetic process
D0008483molecular_functiontransaminase activity
D0009103biological_processlipopolysaccharide biosynthetic process
D0009243biological_processO antigen biosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
D0102933molecular_functionGDP-4-dehydro-6-deoxy-D-mannose-4-aminotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 372
ChainResidue
AGLN213
AARG231
BTYR86
BHOH849

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 372
ChainResidue
CTYR86
CHOH524
DGLN213
DARG231

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 372
ChainResidue
CARG231
DTYR86
DHOH667
CGLN213

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 373
ChainResidue
AGLU294
ALEU296
AHOH435
AHOH455
AHOH594

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AKG A 374
ChainResidue
ATYR86
AASN185
ATRP286
AARG315
AHOH578
BGLN213
BARG231
BHOH909

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q8ZNF3, ECO:0000303|PubMed:18795799
ChainResidueDetails
ALLP186
BLLP186
CLLP186
DLLP186

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
ATYR86
AASP157

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
BTYR86
BASP157

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
CTYR86
CASP157

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
DTYR86
DASP157

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
ASER32

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
BSER32

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
CSER32

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b9h
ChainResidueDetails
DSER32

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PDB entries from 2024-07-10

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