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6NHK

Mortalin nucleotide binding domain in the ADP-bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 501
ChainResidue
ATHR63
AARG391
AASP414
APO4502
AMG503
AHOH605
AASN64
AGLY247
AGLU313
ALYS316
ACYS317
ASER320
AGLY388
AMET389

site_idAC2
Number of Residues8
Detailsbinding site for residue PO4 A 502
ChainResidue
AGLY61
ATHR62
ALYS121
AGLU222
ATHR249
AASP251
AADP501
AMG503

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 503
ChainResidue
AASP244
AADP501
APO4502

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
ATYR196
AASP251
ATHR267
AASN268
AGLY269
AHOH601

site_idAC5
Number of Residues15
Detailsbinding site for residue ADP B 600
ChainResidue
BTHR63
BASN64
BGLY246
BGLY247
BGLU313
BLYS316
BCYS317
BSER320
BGLY387
BGLY388
BMET389
BARG391
BASP414
BPO4601
BMG602

site_idAC6
Number of Residues8
Detailsbinding site for residue PO4 B 601
ChainResidue
BGLY61
BTHR62
BLYS121
BGLU222
BTHR249
BASP251
BADP600
BMG602

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 602
ChainResidue
BASP244
BADP600
BPO4601

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKSEDKVIAvyDL
ChainResidueDetails
AASP233-LEU245

site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS
ChainResidueDetails
AILE58-SER65

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSIL
ChainResidueDetails
AVAL242-LEU255

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGmTRMPkVqQ
ChainResidueDetails
AVAL383-GLN397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30933555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NHK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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