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

7UAI

Meprin alpha helix in complex with fetuin-B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005615cellular_componentextracellular space
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
C0004222molecular_functionmetalloendopeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
D0004222molecular_functionmetalloendopeptidase activity
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0016020cellular_componentmembrane
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
E0008270molecular_functionzinc ion binding
E0016020cellular_componentmembrane
H0004869molecular_functioncysteine-type endopeptidase inhibitor activity
H0005615cellular_componentextracellular space
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IIEHEILHAL
ChainResidueDetails
EILE152-LEU161

site_idPS00740
Number of Residues41
DetailsMAM_1 MAM domain signature. GyFMqfsTssgsaeeaal.LesriLypkrkqqCLqFfYkmtG
ChainResidueDetails
EGLY312-GLY352

site_idPS01254
Number of Residues119
DetailsFETUIN_1 Fetuin family signature 1. CNDsdvlavagfalrdinkdrkdgyvlrlnrvndaqeyrrgglgslfyltldvletdCHvlrkkawqdCgmriffesvygq..CkaifymnnpsrvlylaaynCtlrpvskkkiymtCpdC
ChainResidueDetails
ACYS36-CYS154

site_idPS01255
Number of Residues10
DetailsFETUIN_2 Fetuin family signature 2. DvLETdCHvL
ChainResidueDetails
AASP87-LEU96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER315
HSER315
CGLU156
DGLU156

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN37
DHIS155
DHIS159
DHIS165
AASN136
HASN37
HASN136
BHIS159
BHIS165
CHIS155
CHIS159
CHIS165

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN182
BASN258
BASN414
BASN440
BASN447
BASN539
CASN140
CASN222
CASN258
CASN414
CASN440
HASN182
CASN447
CASN539
DASN140
DASN222
DASN258
DASN414
DASN440
DASN447
DASN539
EASN258
EASN414
EASN440
EASN447
EASN539
BASN140
BASN222

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000250|UniProtKB:Q58D62
ChainResidueDetails
ATHR289
ATHR292
HTHR289
HTHR292

225399

PDB entries from 2024-09-25

PDB statisticsPDBj update infoContact PDBjnumon