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4EZX

Crystal structure of the substrate binding domain of E.coli DnaK in complex with the designer peptide NRLMLTG

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AASN451
ALYS452
ASER453
AHOH935
BASN451
BLYS452
BSER453
BHOH786
BHOH839

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
ASER453
AGLY455
AGLN456
BLYS452

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
AARG467
AASP481
ASER545
ALYS548
AHOH880
AHOH939
AHOH946

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
AARG447
AARG536
AGLU579
BARG447
BHOH773
BHOH824

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 101
ChainResidue
AGLN471
ALYS502
AHOH898
CASN1
CARG2
CHOH207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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