Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QKB

Crystal structure of seleno-methionine labelled human ALKBH7 in complex with alpha-ketoglutarate and Mn(II)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006631biological_processfatty acid metabolic process
A0006974biological_processDNA damage response
A0010883biological_processregulation of lipid storage
A0012501biological_processprogrammed cell death
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A1902445biological_processregulation of mitochondrial membrane permeability involved in programmed necrotic cell death
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006631biological_processfatty acid metabolic process
B0006974biological_processDNA damage response
B0010883biological_processregulation of lipid storage
B0012501biological_processprogrammed cell death
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B1902445biological_processregulation of mitochondrial membrane permeability involved in programmed necrotic cell death
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006631biological_processfatty acid metabolic process
C0006974biological_processDNA damage response
C0010883biological_processregulation of lipid storage
C0012501biological_processprogrammed cell death
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C1902445biological_processregulation of mitochondrial membrane permeability involved in programmed necrotic cell death
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 301
ChainResidue
AHIS121
AASP123
AHIS177
AAKG302

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AKG A 302
ChainResidue
AHIS177
AARG197
ASER199
AARG203
AMN301
AILE70
AHIS108
AHIS121
AASP123
ATYR165

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 303
ChainResidue
AGLU62
AGLU75
BHIS65

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 304
ChainResidue
AGLU189
BGLU189
CGLU189

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 301
ChainResidue
BHIS121
BASP123
BHIS177
BAKG302

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG B 302
ChainResidue
BILE70
BHIS108
BLEU110
BHIS121
BASP123
BMSE143
BTYR165
BHIS177
BARG197
BSER199
BARG203
BMN301

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN B 303
ChainResidue
BGLU62
BGLU75
CHIS65

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN C 301
ChainResidue
CHIS121
CASP123
CHIS177
CAKG302

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AKG C 302
ChainResidue
CHIS108
CLEU110
CHIS121
CASP123
CMSE143
CTYR165
CHIS177
CARG197
CSER199
CARG203
CMN301

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN C 303
ChainResidue
AHIS65
CGLU62
CGLU75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000305|PubMed:25122757
ChainResidueDetails
AHIS121
AASP123
AHIS177
BHIS121
BASP123
BHIS177
CHIS121
CASP123
CHIS177

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ATYR165
AARG203
BTYR165
BARG203
CTYR165
CARG203

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25122757
ChainResidueDetails
AARG197
BARG197
CARG197

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon