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5OOW

Crystal structure of lobe II from the nucleotide binding domain of DnaK in complex with AMPPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ACP A 401
ChainResidue
AGLY196
AGLY342
AGLN343
AHOH522
AGLY197
AGLY198
ATHR199
AGLU267
ALYS270
AILE271
ASER274
AGLY341

site_idAC2
Number of Residues12
Detailsbinding site for residue ACP B 401
ChainResidue
AHOH507
BGLY197
BGLY198
BTHR199
BGLU267
BLYS270
BILE271
BSER274
BGLY342
BGLN343
BARG345
BHOH510

Functional Information from PROSITE/UniProt
site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSII
ChainResidueDetails
AVAL192-ILE205

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK
ChainResidueDetails
AVAL337-LYS351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983
ChainResidueDetails
ATHR199
BTHR199

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS245
ALYS304
BLYS245
BLYS304

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS246
ALYS359
BLYS246
BLYS359

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PDB entries from 2024-09-11

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