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5F2R

Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with AMP-PCP

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 Residues30
Detailsbinding site for residue ACP A 501
ChainResidue
AGLY36
ATHR229
AGLY255
AGLU293
ALYS296
AARG297
ASER300
AGLY363
AGLY364
ASER365
AARG367
ATHR37
AILE368
AMG502
AHOH601
AHOH602
AHOH609
AHOH618
AHOH625
AHOH642
AHOH663
AHOH674
ATHR38
AHOH688
ATYR39
ALYS96
AGLU201
AASP224
AGLY226
AGLY227

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AACP501
AHOH618
AHOH625
AHOH642
AHOH663

site_idAC3
Number of Residues30
Detailsbinding site for residue ACP B 501
ChainResidue
BGLY36
BTHR37
BTHR38
BTYR39
BLYS96
BGLU201
BASP224
BGLY226
BGLY227
BTHR229
BGLY255
BGLU293
BLYS296
BARG297
BSER300
BGLY363
BGLY364
BSER365
BARG367
BILE368
BMG502
BHOH602
BHOH603
BHOH604
BHOH607
BHOH616
BHOH625
BHOH627
BHOH640
BHOH644

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
BACP501
BHOH604
BHOH607
BHOH616
BHOH625

Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS
ChainResidueDetails
AILE33-SER40

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL
ChainResidueDetails
AVAL222-LEU235

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ
ChainResidueDetails
AILE359-GLN373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:21526763
ChainResidueDetails
AGLY36
BGLY364
ALYS96
AGLY227
AGLU293
AGLY364
BGLY36
BLYS96
BGLY227
BGLU293

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761
ChainResidueDetails
ASER86
BSER86

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS125
ALYS213
ALYS326
BLYS125
BLYS213
BLYS326

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ATYR160
BTYR160

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
ALYS271
BLYS271

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029
ChainResidueDetails
ALYS353
BLYS353

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS352
BLYS352

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS353
BLYS353

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PDB entries from 2024-11-06

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