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

6EOM

Structure of DPP III from Caldithrix abyssi

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008239molecular_functiondipeptidyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 601
ChainResidue
AHIS379
AHIS383
AGLU412
AHOH955

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 602
ChainResidue
ALYS55
ALEU201
ATHR231
AILE232

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 603
ChainResidue
ATYR178
ATYR181
AHOH812
AHOH823
ATYR177

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 604
ChainResidue
AGLU53
APRO124
APRO126
APRO134

site_idAC5
Number of Residues4
Detailsbinding site for residue ALA A 605
ChainResidue
ALEU318
AALA319
ALYS606
AHOH938

site_idAC6
Number of Residues7
Detailsbinding site for residue LYS A 606
ChainResidue
AVAL315
ATHR317
ALEU318
ALYS346
AARG450
AALA605
AHOH721

site_idAC7
Number of Residues5
Detailsbinding site for residue NA A 607
ChainResidue
AASP310
ATHR311
AALA313
AVAL315
AHOH949

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLMHEISHGL
ChainResidueDetails
ATHR376-LEU385

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon