From: Detection of protein catalytic residues at high precision using local network properties
Protein | Residues predicted as catalytica | Non-detected catalytic residues | Commentsb |
---|---|---|---|
TEM β-lactamase | Lys73*, Glu166, Asp233, Lys234 | Ser70, Ser130 | Lys234 forms H-bond with substrate analogue-binding water |
Pancreatic phospholipase | Arg6, Glu46, His48, Asp49*, Asp99* | Gly30 | Asp49 binds Ca |
Alkylguanine-transferase | Tyr69, His71, His146*, Arg147, Tyr158, Lys165, Glu172* | Asn137, Cys145 | Glu172→His146 activates Cys145 by deprotonation, Lys165 mutations affect activity |
Ubiquitin-conjugating enzyme 1 | Lys36, Asp55, Asp72 | Cys88 | Detected residues define a single site in structure |
Phenylalanine hydroxylase | His138*, Asp139, His143*, Glu184* | Ser203 | Asp139 forms H-bond with Fe-bound H2O |
Prolyl-isomerase 1 | His59*, Glu145, His157* | Cys113 | Glu145 plays a role in the two-domain arrangement of the protein |
Ferric binding protein | His9*, Glu57*, Arg101, Arg103, Glu144, Glu264 | Tyr195, Tyr196 | Arg101 (not conserved) interacts with ligand, Glu57 interacts with ligand and binds iron |
Bovine β-trypsin | His40, Asp189, Ser190, Asp194, Tyr228, Lys230 | His57, Asp102, Gly193, Gly196, Ser214 | Asp189 forms H-bond with substrate-bound water, Tyr228 is H-bonded to Asp189 through H2O |