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1N2S

CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH

Replaces:  1KC0
Functional Information from GO Data
ChainGOidnamespacecontents
A0000271biological_processpolysaccharide biosynthetic process
A0005829cellular_componentcytosol
A0008831molecular_functiondTDP-4-dehydrorhamnose reductase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
AHOH906
AHOH906
AHOH907
AHOH907
AHOH920
AHOH920

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAI A 901
ChainResidue
AGLN11
AVAL12
AASP30
AVAL31
AGLY38
AASP39
APHE40
AALA62
AALA63
ATHR65
ALEU80
ATYR102
ASER103
ATYR128
ALYS132
ATHR151
AVAL154
AHOH928
AHOH949
AHOH983
AGLY7
ATHR9
AGLY10

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KC1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KC3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Could provide a fine-tuning to achieve optimal pKa matching between active site and substrate","evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATHR104
ATYR106
ATYR128
ALYS132

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATHR104
ALYS132
ATYR128

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PDB entries from 2025-08-27

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