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5LDA

Structure of deubiquitinating enzyme homolog (Pyrococcus furiosus JAMM1) in complex with ubiquitin-like SAMP2.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
AHIS88
AHIS90
AASP101
BGLY69

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL B 601
ChainResidue
AGLU77
BILE9
BLYS42
BGLU61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Glycyl adenylate; alternate => ECO:0000250|UniProtKB:D4GZE7
ChainResidueDetails
BGLY69

site_idSWS_FT_FI2
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2) => ECO:0000250|UniProtKB:D4GZE7
ChainResidueDetails
BLYS55
AHIS90
AASP101

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate => ECO:0000250|UniProtKB:D4GZE7
ChainResidueDetails
ASER98
BGLY69

225158

PDB entries from 2024-09-18

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