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2W3U

formate complex of the Ni-Form of E.coli deformylase

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 NI A 1001
ChainResidue
AGLN50
ACYS90
AHIS132
AHIS136
AFMT1002

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FMT A 1002
ChainResidue
AHIS132
AGLU133
AHIS136
ANI1001
AHOH2095
AHOH2096
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
AGLU133

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9846875
ChainResidueDetails
ACYS90
AHIS132
AHIS136

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLU133
AGLY45
ALEU91
AGLN50

site_idMCSA1
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
AGLY45activator, hydrogen bond acceptor
AGLN50electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ACYS90metal ligand
ALEU91electrostatic stabiliser, hydrogen bond donor
AHIS132metal ligand
AGLU133hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS136metal ligand

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PDB entries from 2024-11-06

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