Structure of PDB 5m4l Chain A

Receptor sequence
>5m4lA (length=484) Species: 9606 (Homo sapiens) [Search protein sequence]
GPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQ
RYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHA
TWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSG
SVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEA
HREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLH
YGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAV
YEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMV
QAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQP
GMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDV
VVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPF
3D structure
PDB5m4l Substrate specificity and reaction mechanism of human prolidase.
ChainA
Resolution1.49 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D60 H255 D276 D287 H366 H370 H377 E412 Y416 R450 E452
Catalytic site (residue number reindexed from 1) D55 H250 D271 D282 H361 H365 H372 E407 Y411 R445 E447
Enzyme Commision number 3.4.13.9: Xaa-Pro dipeptidase.
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 MG A D287 H370 E412 E452 D282 H365 E407 E447
BS02 MG A D276 D287 E452 D271 D282 E447
BS03 OH A D276 D287 E412 E452 D271 D282 E407 E447
BS04 LEU A Y241 H255 D276 D287 H377 Y236 H250 D271 D282 H372
BS05 PRO A H255 H366 H377 R398 E412 R450 H250 H361 H372 R393 E407 R445
Gene Ontology
Molecular Function
GO:0004181 metallocarboxypeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0016805 dipeptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
GO:0102009 proline dipeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006520 amino acid metabolic process
GO:0030574 collagen catabolic process
GO:0043069 negative regulation of programmed cell death
Cellular Component
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5m4l, PDBe:5m4l, PDBj:5m4l
PDBsum5m4l
PubMed28677335
UniProtP12955|PEPD_HUMAN Xaa-Pro dipeptidase (Gene Name=PEPD)

[Back to BioLiP]