1N5N

Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa

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Functional Information from GO Data

ChainGOidnamespacecontents
A0046872molecular_functionmetal ion binding
A0042586molecular_functionpeptide deformylase activity
A0043686biological_processco-translational protein modification
A0031365biological_processN-terminal protein amino acid modification
A0018206biological_processpeptidyl-methionine modification
A0006412biological_processtranslation
B0046872molecular_functionmetal ion binding
B0042586molecular_functionpeptide deformylase activity
B0043686biological_processco-translational protein modification
B0031365biological_processN-terminal protein amino acid modification
B0018206biological_processpeptidyl-methionine modification
B0006412biological_processtranslation
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC15BINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AGLN51
ACYS92
AHIS134
AHIS138
AHOH402

AC25BINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BGLN51
BCYS92
BHIS134
BHIS138
BHOH403

AC37BINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ATYR88
AGLU90
AGLY91
ACYS131
AHIS134
AGOL303
AHOH528

AC47BINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BGLU90
BGLY91
BCYS131
BGLU135
BHOH473
BHOH511
BHOH517

AC57BINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AGLY44
AILE45
AGLY46
AGLY91
ACYS92
ALEU93
AGOL301

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
GOL_1n5n_A_3039GLYCEROL binding site
ChainResidueligand
APRO43-GLY46GOL: GLYCEROL
AGLY91-LEU93GOL: GLYCEROL
ATYR99GOL: GLYCEROL
AGLU135GOL: GLYCEROL

GOL_1n5n_A_30111GLYCEROL binding site
ChainResidueligand
AILE45GOL: GLYCEROL
ATYR88-CYS92GOL: GLYCEROL
ALEU127GOL: GLYCEROL
AVAL130-CYS131GOL: GLYCEROL
AHIS134-GLU135GOL: GLYCEROL

GOL_1n5n_B_30211GLYCEROL binding site
ChainResidueligand
BILE45-GLY46GOL: GLYCEROL
BGLN89-CYS92GOL: GLYCEROL
BLEU127GOL: GLYCEROL
BVAL130-CYS131GOL: GLYCEROL
BHIS134-GLU135GOL: GLYCEROL

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI11By similarity.
ChainResidueDetails
AGLU147

SWS_FT_FI23Iron (By similarity)
ChainResidueDetails
ACYS104
AHIS146
AHIS150

SWS_FT_FI31By similarity.
ChainResidueDetails
BGLU147

SWS_FT_FI43Iron (By similarity)
ChainResidueDetails
BCYS104
BHIS146
BHIS150

extCATRES14Mapped from 1bs4 to 1n5n using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 97272005, 98042282, 99218079
ChainResidueDetails
AGLN50activates substrate. polarises NH of leaving group
AGLU133activates water, cofactor or residue. polarises hydroxide at the Fe centre, assisting nucleophilic atttack on carbonyl group
AGLY45transition-state stabilisation. stabilise negatively charged transition state
ALEU91transition-state stabilisation. stabilise negatively charged transition state

CSA14Annotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLU135
AGLN51
AGLY46
ALEU93

CSA24Annotated By Reference To The Literature 1bs4
ChainResidueDetails
BGLU135
BGLN51
BGLY46
BLEU93

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA14Annotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLU135
AGLN51
AGLY46
ALEU93

CSA24Annotated By Reference To The Literature 1bs4
ChainResidueDetails
BGLU135
BGLN51
BGLY46
BLEU93