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5K8B

X-ray structure of KdnA, 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase, from Shewanella oneidensis in the presence of the external aldimine with PLP and glutamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000271biological_processpolysaccharide biosynthetic process
A0008483molecular_functiontransaminase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0000271biological_processpolysaccharide biosynthetic process
B0008483molecular_functiontransaminase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
C0000271biological_processpolysaccharide biosynthetic process
C0008483molecular_functiontransaminase activity
C0009103biological_processlipopolysaccharide biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
D0000271biological_processpolysaccharide biosynthetic process
D0008483molecular_functiontransaminase activity
D0009103biological_processlipopolysaccharide biosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PDG A 501
ChainResidue
ASER60
AASP183
ALYS186
AHIS325
AHOH613
AHOH645
AHOH686
BARG222
BASN233
BARG235
AGLY61
ATHR62
APHE87
AVAL131
AASP157
ACYS159
AGLN160
ASER181

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 502
ChainResidue
AASN322
ATRP324
AHIS325

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
ALYS262
ASER292

site_idAC4
Number of Residues17
Detailsbinding site for residue PDG B 501
ChainResidue
AARG222
AASN233
AARG235
AHOH636
AHOH713
BSER60
BGLY61
BTHR62
BPHE87
BASP157
BCYS159
BGLN160
BSER181
BASP183
BLYS186
BHIS325
BHOH687

site_idAC5
Number of Residues4
Detailsbinding site for residue CL B 502
ChainResidue
BLYS262
BSER292
BHOH675
BHOH678

site_idAC6
Number of Residues17
Detailsbinding site for residue PDG C 501
ChainResidue
CSER60
CGLY61
CTHR62
CPHE87
CVAL131
CASP157
CCYS159
CGLN160
CSER181
CASP183
CLYS186
CHIS325
CHOH615
CHOH675
DARG222
DASN233
DARG235

site_idAC7
Number of Residues5
Detailsbinding site for residue NA C 502
ChainResidue
CHOH634
CHOH672
CHOH729
CHOH735
DHOH762

site_idAC8
Number of Residues5
Detailsbinding site for residue CL C 503
ChainResidue
CLYS262
CARG278
CPHE290
CSER292
CHOH690

site_idAC9
Number of Residues20
Detailsbinding site for residue PDG D 501
ChainResidue
CARG222
CASN233
CARG235
DSER60
DGLY61
DTHR62
DPHE87
DVAL131
DASP157
DCYS159
DGLN160
DSER181
DASP183
DLYS186
DGLY193
DHIS325
DHOH611
DHOH644
DHOH694
DHOH713

site_idAD1
Number of Residues3
Detailsbinding site for residue CL D 502
ChainResidue
DLYS262
DARG278
DSER292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q8ZNF3
ChainResidueDetails
ALYS186
BLYS186
CLYS186
DLYS186

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PDB entries from 2024-06-19

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