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5NFO

Human JMJD7 in complex with Mn and 2OG in the P21212 form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004177molecular_functionaminopeptidase activity
A0004497molecular_functionmonooxygenase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0018126biological_processprotein hydroxylation
A0035064molecular_functionmethylated histone binding
A0046872molecular_functionmetal ion binding
A0106155molecular_functionpeptidyl-lysine 3-dioxygenase activity
B0004175molecular_functionendopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004497molecular_functionmonooxygenase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0018126biological_processprotein hydroxylation
B0035064molecular_functionmethylated histone binding
B0046872molecular_functionmetal ion binding
B0106155molecular_functionpeptidyl-lysine 3-dioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MN A 501
ChainResidue
AHIS178
AASP180
AHIS277
AAKG502
AHOH680

site_idAC2
Number of Residues14
Detailsbinding site for residue AKG A 502
ChainResidue
AASN184
ATYR186
ALYS193
AHIS277
AVAL279
AASN289
ATRP291
AMN501
AHOH656
AHOH680
ATYR127
ATHR175
AHIS178
AASP180

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
AALA93
AVAL94
AARG95
AGLY118
ASER176
AILE238
APRO239
AHOH661

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 504
ChainResidue
ALYS179
AARG203
ATYR208
APRO236
AASP307
ALYS311
AHOH718

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 505
ChainResidue
ATYR300
AHOH666
BSER-1

site_idAC6
Number of Residues5
Detailsbinding site for residue NO3 A 506
ChainResidue
ASER254
AGLN255
AALA256
AGLN257
AHOH606

site_idAC7
Number of Residues5
Detailsbinding site for residue MN B 501
ChainResidue
BHIS178
BASP180
BHIS277
BAKG502
BHOH680

site_idAC8
Number of Residues14
Detailsbinding site for residue AKG B 502
ChainResidue
BTYR127
BTHR175
BHIS178
BASP180
BASN184
BTYR186
BLYS193
BHIS277
BVAL279
BASN289
BTRP291
BMN501
BHOH645
BHOH680

site_idAC9
Number of Residues9
Detailsbinding site for residue GOL B 503
ChainResidue
ACYS47
BTYR42
BGLU183
BMET294
BGLU295
BASP297
BLYS299
BHOH618
BHOH632

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
BARG203
BTYR208
BPRO236
BASP307
BLYS311

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL B 505
ChainResidue
BALA93
BVAL94
BARG95
BSER176
BILE238
BPRO239
BASP241
BHOH656

site_idAD3
Number of Residues4
Detailsbinding site for residue NO3 B 506
ChainResidue
BGLU104
BARG105
BGLN217
BLEU218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29915238
ChainResidueDetails
AHIS178
AASP180
AHIS277
BHIS178
BASP180
BHIS277

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PDB entries from 2024-09-04

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