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6EOM

Structure of DPP III from Caldithrix abyssi

Functional Information from GO Data
ChainGOidnamespacecontents
A0008239molecular_functiondipeptidyl-peptidase activity
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"O55096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29420664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EOM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

256448

PDB entries from 2026-07-15

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