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

6IFF

Crystal structure of M1 zinc metallopeptidase E323A mutant from Deinococcus radiodurans

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016285molecular_functionalanyl aminopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016285molecular_functionalanyl aminopeptidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
AHIS322
AHIS326
AGLU345
ATYR502

site_idAC2
Number of Residues9
Detailsbinding site for residue TYR A 502
ChainResidue
AHIS326
AGLU345
ATYR396
AZN501
AILE149
AGLU165
AALA301
AGLU303
AHIS322

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
AASP52
AVAL53
AASP181
APRO182
AHOH817
AHOH821

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BHIS322
BHIS326
BGLU345
BTYR502

site_idAC5
Number of Residues10
Detailsbinding site for residue TYR B 502
ChainResidue
BILE149
BGLU165
BALA301
BGLU303
BHIS322
BHIS326
BGLU345
BTYR396
BZN501
BHOH744

site_idAC6
Number of Residues6
Detailsbinding site for residue NA B 503
ChainResidue
BASP52
BVAL53
BASP181
BPRO182
BHOH756
BHOH757

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon