SCOP Family | PDB code of Proteins | Cysteine positions of the SS bond | Sequence Similarity % | Reason for non-conservation | Comment | Ref | |
---|---|---|---|---|---|---|---|
 | with SS | without SS |  |  |  |  |  |
Rubisco, large subunit (c.1.14.1) | 3rub | 8ruc | 172–192 | 94.7 | Crystallographic artifact | Not clear if functionally significant or formed during crystallization period | [83] |
Purple acid phosphatase (d.159.1.1) | 1ute | 1qhw | 163–221 | 84.7 | Crystallographic artifact | No indication crosslink in electron density map | [84] |
VHS domain (a.118.9.2) | 1ujk | 1juq | 33–76 | 72.7 | Crystallographic artifact | Not favorable to accommodate cross link | - |
DnaQ-like 3'-5' exonuclase (c.55.3.5) | 1noy | 1ih7 | 41–55 | 63.9 | Crystallographic artifact | Not favorable to accommodate cross link | - |
Transferrin (c.94.1.2) | - | 1gv8 2tmp | - | - | Fragments of domains | 1gv8 – fragment of N-terminal domain of the intact protein, ovotransferrin 2tmp – only 1–122 residues of N-terminal domain of TIMP | [85] |
Annexin (a.65.1.1) | - | 1scf | - | - | Fragments of domains | Partial structure | - |
G proteins (c.37.1.8) | - | 1ryh 1mh1 1dsb | - | - | Fragments of domains | Partial structure | - |
Glutathione S-transferase, N-terminal domain (c.47.1.5) | 1k0m | 1rk4 | 24–59 | 98.6 | Structural transition | A typical glutathione S-transferase but with a glutaredoxin-like active site. Disulphide bond facilitates a redox-controlled structural transition from monomeric to dimeric state | [49] |
Prion-like (d.6.1.1) | 1i4m | 1uw3 | 179–214 | 91.2 | Structural transition | Rearrangement of disulphide bonds helps in conformationallly altering the prion protein to pathogenic oligomeric form. | [50] |
Alpha-macroglobulin receptor domain (b.2.4.1) | 1ayo/1bv8 | 1edy | 17–132 | 66.2 | Structural transition | Major conformational differences between human/bovine and rat RBD | [60] |
Papain-like (d.3.1.1) | 1qdq | 3pbh | 148–252 | 88.9 | Stabilization of local structure | Disulphide bond increases the conformational flexibility of the occluding loop, although the conformational stability of the overall structure is little affected. | [54] |
Parvalbumin (a.39.1.4) | 1a75 | 1bu3 | 11–33 | 88.7 | Stabilization of local structure | This disulphide bond is unique to Whiting parvalbumin and stabilizes the two helical hairpin although the conformational stability of the overall structure is little affected. | - |
Dipeptidyl peptidase IV/CD26, N-terminal domain (b.70.3.1) | 1nu6 | 1orv | 328–339 | 85.7 | Increased activity | Adenosine deaminase (ADA) binds stronger to the disulphide bonded human protein than in porcine. | [51] |
Ricin B-like (b.42.2.1) | 2aai | 1m2t 1onk | 20–39 | 72.6 | Increased activity | Reduced cytotoxicity in mistle toe lectin | [52] |
Xylanase/endoglucanase 11/12 (b.29.1.11) | 1yna | 1xnd | 110–154 | 59.5 | Increased activity | Increased thermostability due to compounding effect of disulphide bond with increase in the density of charged particles | [53] |
Mycobacterial antigens (c.69.1.3) | 1f0n | 1dqz | 87–92 | 72.1 | Unassigned role | Not obvious from the structural differences if the antigens have different biological roles | [55] |
Quinoprotein alcohol dehydrogenase-like (b.70.1.1) | 1g72 | 1kb0 1kb9 | 144–167 | 33.2 | Unassigned role | No structural or functional role assigned | [56] |
Subtilases (c.41.1.1) | 1dbi | 1thm | 137–139 | 61.6 | Unassigned role | C-X-C disulphide bridge is hypothesised to enhance the thermaostability | [57] |
Hemorrhagin (d.92.1.9) | 1bud | 4aig | 157–164 | 49.2 | Unassigned role | No direct evidence if the variable disulphide bridges in the C-terminal subdomain hemorrhagin family of enzymes lead to differences in their hemorrhagic activity. | [58] |