Structure of PDB 4nff Chain A

Receptor sequence
>4nffA (length=229) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGWECEKHSQPWQVAVYSHGWAHCGGVLVHPQWVLTAAHCLKKNSQVW
LGRHNLFEPEDTGQRVPVSHSFPHPLYNMSLLEDSSHDLMLLRLSEPAKI
TDVVKVLGLPTQEPALGTTCYASGWGSIEPEEFLRPRSLQCVSLHLLSND
MCARAYSEKVTEFMLCAGLWTGGKDTCGGDSGGPLVCNGVLQGITSWGPE
PCALPEKPAVYTKVVHYRKWIKDTIAANP
3D structure
PDB4nff Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 G192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H41 D88 G178 G179 D180 S181 G182
Enzyme Commision number 3.4.21.35: tissue kallikrein.
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 0G6 A H57 E174 D189 T190 C191 G193 S195 S214 W215 G216 P217 C220 H41 E158 D175 T176 C177 G179 S181 S196 W197 G198 P199 C202
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region
GO:0030141 secretory granule
GO:0070062 extracellular exosome

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Biological Process
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Cellular Component
External links
PDB RCSB:4nff, PDBe:4nff, PDBj:4nff
PDBsum4nff
PubMed25326387
UniProtP20151|KLK2_HUMAN Kallikrein-2 (Gene Name=KLK2)

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