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5FNC

Dynamic Undocking and the Quasi-Bound State as tools for Drug Design

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IEE A 1225
ChainResidue
AALA55
ATHR184
AHOH2048
AHOH2088
AASP93
AILE96
AGLY97
AMET98
ALEU107
AALA111
AGLY135
APHE138

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1226
ChainResidue
AASP54
AASP54

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1227
ChainResidue
APHE22
AGLN23
AILE26
AGLY108
AHOH2104

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1228
ChainResidue
AHIS77
AASN79
AHOH2128

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR38-GLU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASN51
AASP93
APHE138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541
ChainResidueDetails
ATHR5
ATHR7

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS58
ALYS84

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER231

226707

PDB entries from 2024-10-30

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