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1BUP

T13S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 487
ChainResidue
AADP486
APO4488
AK490
AHOH560
AHOH561
AHOH562
AHOH563

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 490
ChainResidue
AADP486
AMG487
AHOH558
AHOH562
AHOH563
AASP10
ATYR15

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 491
ChainResidue
AASP199
ATHR204
AASP206
APO4488
AHOH560

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 451
ChainResidue
ATYR183
ALYS345
ALYS348
AHOH523
AHOH537

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 828
ChainResidue
AASN31
AASP32
AGLN33
ALYS126

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PO4 A 488
ChainResidue
AGLY12
ASER13
ALYS71
APRO147
AGLU175
ATHR204
AADP486
AMG487
AK491
AHOH509
AHOH545
AHOH560
AHOH561
AHOH562

site_idAC7
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ADP A 486
ChainResidue
AGLY12
ASER13
ATHR14
ATYR15
AGLY201
AGLY202
AGLY230
AGLU268
ALYS271
AARG272
ASER275
AGLY339
ASER340
AARG342
AILE343
AASP366
AMG487
APO4488
AK490
AHOH545
AHOH547
AHOH558
AHOH560
AHOH562
AHOH563
AHOH564
AHOH587
AHOH799
AHOH1053

Functional Information from PROSITE/UniProt
site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL
ChainResidueDetails
AILE197-LEU210

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK
ChainResidueDetails
AILE334-LYS348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY12
ALYS71

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0007744|PDB:2QWL, ECO:0007744|PDB:2QWM, ECO:0007744|PDB:2QWN, ECO:0007744|PDB:2QWO, ECO:0007744|PDB:2QWP, ECO:0007744|PDB:2QWQ
ChainResidueDetails
ATHR14
ATYR15
AGLY202
AGLU268
ALYS271
ASER275
AGLY339

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11142
ChainResidueDetails
ASER2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
ALYS108
ALYS328

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11142
ChainResidueDetails
ASER153
ASER329
ASER362

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11142
ChainResidueDetails
ALYS246

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P63017
ChainResidueDetails
ALYS319

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kaz
ChainResidueDetails
ALYS71

site_idMCSA1
Number of Residues4
DetailsM-CSA 656
ChainResidueDetails
AASP10
ALYS71enhance reactivity
AGLU175
AASP199

227344

PDB entries from 2024-11-13

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