7UAI
Meprin alpha helix in complex with fetuin-B
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
A | 0005615 | cellular_component | extracellular space |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016020 | cellular_component | membrane |
C | 0004222 | molecular_function | metalloendopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016020 | cellular_component | membrane |
D | 0004222 | molecular_function | metalloendopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016020 | cellular_component | membrane |
E | 0004222 | molecular_function | metalloendopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008270 | molecular_function | zinc ion binding |
E | 0016020 | cellular_component | membrane |
H | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
H | 0005615 | cellular_component | extracellular space |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IIEHEILHAL |
Chain | Residue | Details |
E | ILE152-LEU161 |
site_id | PS00740 |
Number of Residues | 41 |
Details | MAM_1 MAM domain signature. GyFMqfsTssgsaeeaal.LesriLypkrkqqCLqFfYkmtG |
Chain | Residue | Details |
E | GLY312-GLY352 |
site_id | PS01254 |
Number of Residues | 119 |
Details | FETUIN_1 Fetuin family signature 1. CNDsdvlavagfalrdinkdrkdgyvlrlnrvndaqeyrrgglgslfyltldvletdCHvlrkkawqdCgmriffesvygq..CkaifymnnpsrvlylaaynCtlrpvskkkiymtCpdC |
Chain | Residue | Details |
A | CYS36-CYS154 |
site_id | PS01255 |
Number of Residues | 10 |
Details | FETUIN_2 Fetuin family signature 2. DvLETdCHvL |
Chain | Residue | Details |
A | ASP87-LEU96 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER315 | |
H | SER315 | |
C | GLU156 | |
D | GLU156 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
Chain | Residue | Details |
A | ASN37 | |
D | HIS155 | |
D | HIS159 | |
D | HIS165 | |
A | ASN136 | |
H | ASN37 | |
H | ASN136 | |
B | HIS159 | |
B | HIS165 | |
C | HIS155 | |
C | HIS159 | |
C | HIS165 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN182 | |
B | ASN258 | |
B | ASN414 | |
B | ASN440 | |
B | ASN447 | |
B | ASN539 | |
C | ASN140 | |
C | ASN222 | |
C | ASN258 | |
C | ASN414 | |
C | ASN440 | |
H | ASN182 | |
C | ASN447 | |
C | ASN539 | |
D | ASN140 | |
D | ASN222 | |
D | ASN258 | |
D | ASN414 | |
D | ASN440 | |
D | ASN447 | |
D | ASN539 | |
E | ASN258 | |
E | ASN414 | |
E | ASN440 | |
E | ASN447 | |
E | ASN539 | |
B | ASN140 | |
B | ASN222 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000250|UniProtKB:Q58D62 |
Chain | Residue | Details |
A | THR289 | |
A | THR292 | |
H | THR289 | |
H | THR292 |