Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) Binds 1 Ca(2+) ion. Oxyphenbutazone (OPB), anisic acid and atropine inhibit the enzymatic activity by binding at the substrate-binding site (PubMed:15544328, PubMed:16596639). P-coumaric acid, resveratrol, spermidine, corticosterone and gramine derivative inhibit the enzymatic activity by binding at the substrate-binding site (PubMed:25541253). Monomer. Expressed by the venom gland. LD(50) is between 5.3 and 5.5 mg/kg by intravenous injection into mice. D.russelli pulchella is synonymous with D.russelii. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.