Vol. I · An interactive catalogue of biological machines

The quiet machinery of life, rendered legibly.

Each entry pairs a photo-real three-dimensional structure with its catalytic cycle, its kinetic signature, and the vibrational modes that drive allostery. You can rotate, mutate, integrate — all in the browser, with the citations kept honest.

100% client-sideDynamics in < 1 sMol★ structures from RCSB
01

Mechanism, step by step

Curated catalytic cycles — key residues, transition states, rate-limiting steps — sourced from M-CSA and primary literature, not hand-waved.

02

Kinetics from the record

kcat, KM, kcat/KM, pH, temperature, and source for every entry, with a live RK4 integrator that lets you inhibit and observe.

03

Dynamics computed here

Upload any PDB and get normal modes, cross-correlations, and a steered elastic-network response in seconds — entirely in your browser.

§ Catalog

Classic enzymes, chosen with care.

Each enzyme in the catalogue earns its place by pedagogical depth, structural clarity, and the availability of kinetic and mechanistic data — the ingredients needed to understand, not merely depict.

6 entries · updated quarterly
EC EC 3.2.1.17

Lysozyme

1AKI
Gallus gallus

The archetype of mechanistic enzymology. Cleaves β-1,4 glycosidic bonds in bacterial peptidoglycan through an oxocarbenium-ion intermediate.

glycoside hydrolaseoxocarbeniumretainingmonomeric
Hydrolase / glycosidase129 aa · 1 chain
EC EC 5.3.1.1

TIM

1YPI
Saccharomyces cerevisiae

A catalytically perfect enzyme — its reaction is limited only by diffusion. Interconverts GAP and DHAP via a cis-enediol(ate) intermediate.

isomeraseTIM barrelloop dynamicsdiffusion-limited
Isomerase247 aa · 2 chains
EC EC 3.4.21.1

Chymotrypsin

4CHA
Bos taurus

The paradigm of the catalytic triad (Ser-His-Asp). Two-step mechanism: acylation forms a covalent acyl-enzyme intermediate; deacylation by water releases the C-terminal product.

serine proteasecatalytic triadcovalentacyl-enzyme
Hydrolase / serine protease241 aa · 3 chains
EC EC 4.2.1.1

CA II

3KS3
Homo sapiens

One of the fastest enzymes known (kcat ≈ 10⁶ s⁻¹). Catalyses the reversible hydration of CO₂ to bicarbonate via a zinc-hydroxide mechanism.

metalloenzymezinclyaseproton wire
Lyase / metalloenzyme260 aa · 1 chain
EC EC 3.4.23.16

HIV-1 PR

1HVR
Human immunodeficiency virus type 1

Obligate homodimer where each subunit contributes one Asp25 to a shared catalytic dyad. Hydrolyses viral polyproteins into functional proteins — essential for HIV maturation.

aspartyl proteasehomodimerdrug targetHIV
Hydrolase / aspartyl protease198 aa · 2 chains
EC EC 3.4.22.69

Mpro

6LU7
SARS-CoV-2

Cysteine-histidine catalytic dyad. Cleaves the coronaviral polyprotein at 11 conserved Leu-Gln↓(Ser/Ala/Gly) sites — essential for viral replication.

cysteine proteasecoronavirusdrug targetcovalent inhibitor
Hydrolase / cysteine protease306 aa · 1 chain