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1VQ0

Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0042026biological_processprotein refolding
A0044183molecular_functionprotein folding chaperone
A0051082molecular_functionunfolded protein binding
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0042026biological_processprotein refolding
B0044183molecular_functionprotein folding chaperone
B0051082molecular_functionunfolded protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
ACYS231
ACYS233
ACYS263
ACYS266

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BCYS231
BCYS233
BCYS263
BCYS266

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AMET19
AALA168
AARG18

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 301
ChainResidue
BARG18
BALA168

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE UNL A 302
ChainResidue
ACYS231
ACYS233
AASN234
AARG235
ATHR268
ATYR270
AHOH308
AHOH313
AHOH366
AHOH399
BLEU96
BHOH327

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UNL B 302
ChainResidue
ALEU96
BCYS231
BCYS233
BASN234
BARG235
BTHR268
BTYR270
BHOH306
BHOH318
BHOH357
BHOH358

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BARG13
BTRP60
BPHE144
BGLU148

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AARG13
ATRP60
APHE144
AGLU148

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
AGLN110
BLYS122

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PDB entries from 2025-06-11

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