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1NLT

The crystal structure of Hsp40 Ydj1

Functional Information from GO Data
ChainGOidnamespacecontents
A0006457biological_processprotein folding
A0030544molecular_functionHsp70 protein binding
A0031072molecular_functionheat shock protein binding
A0051082molecular_functionunfolded protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 351
ChainResidue
ACYS143
AGLU145
ACYS146
ACYS201
ACYS204

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 352
ChainResidue
ACYS159
ACYS162
ACYS185
ACYS188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues83
DetailsZN_FING: CR-type
ChainResidueDetails
AGLY130-ARG213

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AILE116
ACYS204
AILE215
AVAL247
ALEU135
ACYS143
ACYS146
ACYS159
ACYS162
ACYS185
ACYS188
ACYS201

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Involved in dimerization
ChainResidueDetails
AASP335

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS198

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PDB entries from 2024-07-24

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