Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6LGK

Crystal structure of an oxido-reductase with mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0002376biological_processimmune system process
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0006915biological_processapoptotic process
A0008017molecular_functionmicrotubule binding
A0015630cellular_componentmicrotubule cytoskeleton
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0016740molecular_functiontransferase activity
A0017148biological_processnegative regulation of translation
A0019899molecular_functionenzyme binding
A0031906cellular_componentlate endosome lumen
A0032481biological_processpositive regulation of type I interferon production
A0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
A0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043209cellular_componentmyelin sheath
A0045087biological_processinnate immune response
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0050661molecular_functionNADP binding
A0050821biological_processprotein stabilization
A0051287molecular_functionNAD binding
A0051402biological_processneuron apoptotic process
A0061621biological_processcanonical glycolysis
A0097452cellular_componentGAIT complex
B0000226biological_processmicrotubule cytoskeleton organization
B0002376biological_processimmune system process
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006006biological_processglucose metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0006915biological_processapoptotic process
B0008017molecular_functionmicrotubule binding
B0015630cellular_componentmicrotubule cytoskeleton
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0016740molecular_functiontransferase activity
B0017148biological_processnegative regulation of translation
B0019899molecular_functionenzyme binding
B0031906cellular_componentlate endosome lumen
B0032481biological_processpositive regulation of type I interferon production
B0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
B0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043209cellular_componentmyelin sheath
B0045087biological_processinnate immune response
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0050661molecular_functionNADP binding
B0050821biological_processprotein stabilization
B0051287molecular_functionNAD binding
B0051402biological_processneuron apoptotic process
B0061621biological_processcanonical glycolysis
B0097452cellular_componentGAIT complex
C0000226biological_processmicrotubule cytoskeleton organization
C0002376biological_processimmune system process
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0006006biological_processglucose metabolic process
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0006417biological_processregulation of translation
C0006915biological_processapoptotic process
C0008017molecular_functionmicrotubule binding
C0015630cellular_componentmicrotubule cytoskeleton
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0016740molecular_functiontransferase activity
C0017148biological_processnegative regulation of translation
C0019899molecular_functionenzyme binding
C0031906cellular_componentlate endosome lumen
C0032481biological_processpositive regulation of type I interferon production
C0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
C0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0043209cellular_componentmyelin sheath
C0045087biological_processinnate immune response
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0050661molecular_functionNADP binding
C0050821biological_processprotein stabilization
C0051287molecular_functionNAD binding
C0051402biological_processneuron apoptotic process
C0061621biological_processcanonical glycolysis
C0097452cellular_componentGAIT complex
D0000226biological_processmicrotubule cytoskeleton organization
D0002376biological_processimmune system process
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0006006biological_processglucose metabolic process
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0006417biological_processregulation of translation
D0006915biological_processapoptotic process
D0008017molecular_functionmicrotubule binding
D0015630cellular_componentmicrotubule cytoskeleton
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0016740molecular_functiontransferase activity
D0017148biological_processnegative regulation of translation
D0019899molecular_functionenzyme binding
D0031906cellular_componentlate endosome lumen
D0032481biological_processpositive regulation of type I interferon production
D0035605molecular_functionpeptidyl-cysteine S-nitrosylase activity
D0035606biological_processpeptidyl-cysteine S-trans-nitrosylation
D0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
D0043209cellular_componentmyelin sheath
D0045087biological_processinnate immune response
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0050661molecular_functionNADP binding
D0050821biological_processprotein stabilization
D0051287molecular_functionNAD binding
D0051402biological_processneuron apoptotic process
D0061621biological_processcanonical glycolysis
D0097452cellular_componentGAIT complex
Functional Information from PDB Data
site_idAC1
Number of Residues39
Detailsbinding site for residue NAD A 401
ChainResidue
AASN9
APHE37
AILE38
AARG80
ASER98
ATHR99
AGLY100
APHE102
ASER122
AALA123
AALA183
AGLY10
AASN316
ATYR320
APO4403
AHOH503
AHOH512
AHOH528
AHOH553
AHOH560
AHOH569
AHOH585
APHE11
AHOH588
AHOH595
AHOH627
AHOH657
AHOH662
AHOH670
AHOH704
AHOH711
AHOH715
BPRO191
AGLY12
AARG13
AILE14
AASN34
AASP35
APRO36

site_idAC2
Number of Residues12
Detailsbinding site for residue PO4 A 402
ChainResidue
ASER151
ASER152
ATHR153
AHIS179
ATHR211
AGLY212
APO4403
AHOH560
AHOH577
AHOH588
AHOH647
AHOH653

site_idAC3
Number of Residues7
Detailsbinding site for residue PO4 A 403
ChainResidue
ATHR182
ATHR184
AARG234
ANAD401
APO4402
AHOH503
AHOH510

site_idAC4
Number of Residues37
Detailsbinding site for residue NAD B 401
ChainResidue
BASN9
BGLY10
BPHE11
BGLY12
BARG13
BILE14
BASN34
BASP35
BPRO36
BPHE37
BILE38
BGLU79
BARG80
BSER98
BTHR99
BGLY100
BPHE102
BSER122
BALA123
BALA183
BASN316
BTYR320
BPO4403
BHOH504
BHOH506
BHOH515
BHOH518
BHOH528
BHOH592
BHOH636
BHOH643
BHOH661
BHOH665
BHOH691
BHOH701
BHOH713
BHOH715

site_idAC5
Number of Residues12
Detailsbinding site for residue PO4 B 402
ChainResidue
BTHR211
BGLY212
BPO4403
BHOH526
BHOH528
BHOH540
BHOH603
BHOH692
BSER151
BSER152
BTHR153
BHIS179

site_idAC6
Number of Residues6
Detailsbinding site for residue PO4 B 403
ChainResidue
BTHR182
BTHR184
BARG234
BNAD401
BPO4402
BHOH504

site_idAC7
Number of Residues34
Detailsbinding site for residue NAD C 401
ChainResidue
CASN9
CGLY10
CPHE11
CGLY12
CARG13
CILE14
CASN34
CASP35
CPRO36
CPHE37
CARG80
CSER98
CTHR99
CGLY100
CPHE102
CSER122
CALA123
CALA183
CASN316
CTYR320
CPO4403
CHOH508
CHOH510
CHOH526
CHOH531
CHOH541
CHOH618
CHOH634
CHOH636
CHOH649
CHOH655
CHOH679
CHOH696
CHOH706

site_idAC8
Number of Residues11
Detailsbinding site for residue PO4 C 402
ChainResidue
CSER151
CSER152
CTHR153
CTHR211
CGLY212
CALA213
CPO4403
CHOH544
CHOH610
CHOH660
CHOH711

site_idAC9
Number of Residues8
Detailsbinding site for residue PO4 C 403
ChainResidue
CTHR182
CTHR184
CLYS194
CARG234
CNAD401
CPO4402
CHOH508
CHOH665

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues580
DetailsRegion: {"description":"Interaction with WARS1","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsMotif: {"description":"[IL]-x-C-x-x-[DE] motif","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsModified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues32
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues24
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"UniProtKB","id":"P04797","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P04406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon