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3EDH

Crystal structure of bone morphogenetic protein 1 protease domain in complex with partially bound DMSO

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACE A 201
ChainResidue
AALA1
AALA2
AGLU103
AARG106
ASER136
AGLN189

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 210
ChainResidue
AHIS92
AHIS96
AHIS102

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 211
ChainResidue
AGLU103
AGLN189
AHOH221
AHOH224
AHOH228

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 212
ChainResidue
ALYS39
AHIS40
AARG106
AASP108
AGLU139
AHOH290
AHOH581

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 213
ChainResidue
AARG35
ALYS39
ALYS192
AHOH462
AHOH594

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DMS A 214
ChainResidue
ACYS64
AHIS92
AGLU93
AHIS96
AHIS102
AHOH297
AHOH306
AHOH314
AHOH604
AHOH609

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 215
ChainResidue
AASP50
AARG176
ATHR180
AHOH536

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 216
ChainResidue
AARG31
AGLU38
APHE45
AHOH546

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IVVHELGHVV
ChainResidueDetails
AILE89-VAL98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues199
DetailsDomain: {"description":"Peptidase M12A","evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ast
ChainResidueDetails
ATYR149
AGLU93

242199

PDB entries from 2025-09-24

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