Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2IXJ

RmlC P aeruginosa native

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008830molecular_functiondTDP-4-dehydrorhamnose 3,5-epimerase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009244biological_processlipopolysaccharide core region biosynthetic process
A0016853molecular_functionisomerase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SRT A1185
ChainResidue
AARG62
AHOH2067
AHOH2085
AHOH2086
AHOH2087
AHIS65
ALYS74
AARG92
AHIS121
ATYR134
ATRP140
AGLU145
AHOH2029

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17046787
ChainResidueDetails
AHIS65

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:17046787
ChainResidueDetails
ATYR134

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXK
ChainResidueDetails
AARG26
AGLU31

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXH
ChainResidueDetails
AGLN50

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK
ChainResidueDetails
AARG62

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK
ChainResidueDetails
ALYS74
AHIS121

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXJ
ChainResidueDetails
AGLU145

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXK
ChainResidueDetails
ALYS170

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1
ChainResidueDetails
ATRP140

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dzr
ChainResidueDetails
AHIS65
AASP171

site_idMCSA1
Number of Residues4
DetailsM-CSA 329
ChainResidueDetails
AHIS65proton acceptor, proton donor
ALYS74electrostatic stabiliser
ATYR134proton acceptor, proton donor, proton relay
AASP171electrostatic stabiliser, increase acidity, increase basicity

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon