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5IAA

Crystal structure of human UBA5 in complex with UFM1

Functional Information from GO Data
ChainGOidnamespacecontents
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0007420biological_processbrain development
C0033146biological_processregulation of intracellular estrogen receptor signaling pathway
C0034976biological_processresponse to endoplasmic reticulum stress
C0042308biological_processnegative regulation of protein import into nucleus
C0043066biological_processnegative regulation of apoptotic process
C0061709biological_processreticulophagy
C0071569biological_processprotein ufmylation
C1990592biological_processprotein K69-linked ufmylation
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0007420biological_processbrain development
D0033146biological_processregulation of intracellular estrogen receptor signaling pathway
D0034976biological_processresponse to endoplasmic reticulum stress
D0042308biological_processnegative regulation of protein import into nucleus
D0043066biological_processnegative regulation of apoptotic process
D0061709biological_processreticulophagy
D0071569biological_processprotein ufmylation
D1990592biological_processprotein K69-linked ufmylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS226
ACYS229
ACYS303
ACYS308

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS226
BCYS229
BCYS303
BCYS308

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues29
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VAIVGvGGVGsvtaemltrcgigkLLlFD
ChainResidueDetails
AVAL76-ASP104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1) => ECO:0000269|PubMed:25219498
ChainResidueDetails
CLYS69
DLYS69

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000269|PubMed:15071506, ECO:0000269|PubMed:25219498, ECO:0000269|PubMed:27653677
ChainResidueDetails
AGLY83
CGLY83
AASN150
DGLY83
BGLY83
BLYS127
BASN150
BASN184

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20368332, ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706, ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H78
ChainResidueDetails
AASP104
BASP104

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20368332, ECO:0000269|PubMed:27653677, ECO:0000269|PubMed:30412706, ECO:0007744|PDB:5IAA, ECO:0007744|PDB:5L95, ECO:0007744|PDB:6H77, ECO:0007744|PDB:6H78
ChainResidueDetails
ACYS226
ACYS229
ACYS303
ACYS308
BCYS226
BCYS229
BCYS303
BCYS308

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PDB entries from 2024-11-06

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