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4QU2

The structure of JMJD7 with alpha-KG

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004177molecular_functionaminopeptidase activity
A0004497molecular_functionmonooxygenase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0035064molecular_functionmethylated histone binding
A0046872molecular_functionmetal ion binding
A0106155molecular_functionpeptidyl-lysine 3-dioxygenase activity
B0004175molecular_functionendopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004497molecular_functionmonooxygenase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0035064molecular_functionmethylated histone binding
B0046872molecular_functionmetal ion binding
B0106155molecular_functionpeptidyl-lysine 3-dioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 501
ChainResidue
AHIS178
AASP180
AHIS277
AAKG502

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG A 502
ChainResidue
ATYR186
ALYS193
AHIS277
AVAL279
ATRP291
ANI501
AHOH612
ATYR127
ATRP167
ATHR175
AHIS178
AASN184

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 501
ChainResidue
BGLN131
BHIS178
BASP180
BHIS277
BAKG502

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AKG B 502
ChainResidue
BTYR127
BTRP167
BTHR175
BHIS178
BASP180
BASN184
BTYR186
BLYS193
BHIS277
BVAL279
BASN289
BNI501
BHOH611
BHOH624

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538
ChainResidueDetails
AHIS178
AASP180
AHIS277
BHIS178
BASP180
BHIS277

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PDB entries from 2024-06-12

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