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6ZMD

Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0140662molecular_functionATP-dependent protein folding chaperone
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. VFDLGGGAfdvSLL
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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942
ChainResidueDetails
BHIS363
ALYS96
AGLY227
AGLU293
AGLY364

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U
ChainResidueDetails
BGLY234

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U
ChainResidueDetails
BVAL316
BTYR399
BASN407

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07
ChainResidueDetails
BASP367

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325
ChainResidueDetails
BGLY234

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083
ChainResidueDetails
BALA183

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083
ChainResidueDetails
BASN275

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8
ChainResidueDetails
AARG492

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; alternate => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR518

site_idSWS_FT_FI10
Number of Residues1
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

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS353

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PDB entries from 2024-11-06

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