Structure of PDB 4gwm Chain B

Receptor sequence
>4gwmB (length=554) Species: 9606 (Homo sapiens) [Search protein sequence]
PWENFDVDGGMDQDIFDINEGLGLDLFEGDIRLDRAQIRNSIIGEKYRWP
HTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWAGETNYISVFKGS
GCWSSVGNRRVGKQELSIGANCDRIATVQHEFLHALGFWHEQSRSDRDDY
VRIMWDRILSGREHNFNTLNVPYDYTSVMHYSKTAFQNGTEPTIVTRISD
FEDVIGQRMDFSDSDLLKLNQLYNCSSSLSFMDSCSFELENVCGMIQNAD
WQRVSQVPRGPESDHSNGSGFFMHFDSSSVNVGATAVLESRTLYPKRGFQ
CLQFYLYNSGSESDQLNIYIREYSADNVDGNLTLVEEIKEIPTGSWQLYH
VTLKVTKKFRVVFEGRKGSGASLGGLSIDDINLSETRCPHHIWHIRNFTQ
FIGSPNGTLYSPPFYSSKGYAFQIYLNLAHVTNAGIYFHLISGANDDQLQ
WPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPFMTTDNGNYFWDRPSKV
GTVALFSNGTQFRRGGGYGTSAFITHERLKSRDFIKGDDVYILLTVEDIS
HLNS
3D structure
PDB4gwm Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H152 E153 H156 H162 Y211
Catalytic site (residue number reindexed from 1) H130 E131 H134 H140 Y181
Enzyme Commision number 3.4.24.63: meprin B.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MAN B Y454 N484 Y415 N445
BS02 MAN B S456 K457 S417 K418
BS03 MAN B N484 Q487 N445 Q448
BS04 ZN B D52 H152 H156 H162 D30 H130 H134 H140
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4gwm, PDBe:4gwm, PDBj:4gwm
PDBsum4gwm
PubMed22988105
UniProtQ16820|MEP1B_HUMAN Meprin A subunit beta (Gene Name=MEP1B)

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