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1XEO

High Resolution Crystals Structure of Cobalt- Peptide Deformylase Bound To Formate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0042586molecular_functionpeptide deformylase activity
A0043022molecular_functionribosome binding
A0043686biological_processco-translational protein modification
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 301
ChainResidue
AGLN50
ACYS90
AHIS132
AHIS136
AFMT401

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 401
ChainResidue
AHIS132
AGLU133
AHIS136
ACO301
AGLY45
AGLN50
ACYS90
ALEU91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9846875
ChainResidueDetails
AMET134

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9846875
ChainResidueDetails
ALEU91
AGLU133
ALEU137

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
AVAL51electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ALEU91metal ligand
ASER92electrostatic stabiliser, hydrogen bond donor
AGLU133metal ligand
AMET134hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALEU137metal ligand
ALEU46activator, hydrogen bond acceptor

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PDB entries from 2024-06-12

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