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5HPH

Structure of TRAP1 fragment

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
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue ANP A 801
ChainResidue
AGLU115
AGLY199
AGLN200
APHE201
AGLY202
AVAL203
AGLY204
APHE205
ATHR251
AARG402
AMG803
AASN119
AHOH905
AHOH912
AHOH913
AHOH916
AALA123
ALYS126
AASP158
AASN171
ASER178
AGLY179
ASER180

site_idAC2
Number of Residues3
Detailsbinding site for residue PO4 A 802
ChainResidue
ATYR331
AARG421
AHOH935

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 803
ChainResidue
AASN119
AANP801
AHOH912

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 804
ChainResidue
ASER266
AGLU267
AALA268

site_idAC5
Number of Residues1
Detailsbinding site for residue SO4 A 805
ChainResidue
AGLN406

site_idAC6
Number of Residues26
Detailsbinding site for residue ANP B 801
ChainResidue
BGLU115
BASN119
BALA123
BLYS126
BASP158
BMET163
BASN171
BSER178
BGLY179
BSER180
BGLY199
BGLN200
BPHE201
BGLY202
BVAL203
BGLY204
BPHE205
BTHR251
BARG402
BMG805
BHOH903
BHOH917
BHOH918
BHOH931
BHOH937
BHOH946

site_idAC7
Number of Residues2
Detailsbinding site for residue PO4 B 802
ChainResidue
BTYR331
BARG421

site_idAC8
Number of Residues7
Detailsbinding site for residue PO4 B 803
ChainResidue
BPRO350
BASP354
BLEU359
BARG385
BPHE386
BARG388
BPHE447

site_idAC9
Number of Residues7
Detailsbinding site for residue SO4 B 804
ChainResidue
AGLN406
AGLU407
BALA102
BARG103
BTYR106
BMET210
BHOH905

site_idAD1
Number of Residues3
Detailsbinding site for residue MG B 805
ChainResidue
BASN119
BANP801
BHOH918

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 806
ChainResidue
AALA176
AARG177
ASER178
ALYS181
BGLU93
BLYS96

site_idAD3
Number of Residues3
Detailsbinding site for residue GOL B 807
ChainResidue
BSER265
BGLU267
BALA268

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL B 808
ChainResidue
AGLU93
ALYS96
BALA176
BARG177
BSER178
BLYS181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN119
BARG402
AASP158
AASN171
APHE205
AARG402
BASN119
BASP158
BASN171
BPHE205

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5XHZ0
ChainResidueDetails
ASER170
BSER170

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5XHZ0
ChainResidueDetails
ATHR174
BTHR174

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER194
BSER194

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQN1
ChainResidueDetails
ALYS262
ALYS324
ALYS431
BLYS262
BLYS324
BLYS431

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS332
ALYS424
ALYS466
BLYS332
BLYS424
BLYS466

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR494
BTHR494

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PDB entries from 2024-07-03

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