5KHU
Model of human Anaphase-promoting complex/Cyclosome (APC15 deletion mutant), in complex with the Mitotic checkpoint complex (APC/C-CDC20-MCC) based on cryo EM data at 4.8 Angstrom resolution
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Anaphase-promoting complex subunit 1 | polymer | 1944 | 217580.2 | 1 | UniProt (Q9H1A4) Pfam (PF12859) Pfam (PF20518) Pfam (PF21282) Pfam (PF18122) In PDB | Homo sapiens (Human) | APC1,Cyclosome subunit 1,Mitotic checkpoint regulator,Testis-specific gene 24 protein |
2 | B | Anaphase-promoting complex subunit 11 | polymer | 84 | 9854.6 | 1 | UniProt (Q9NYG5) Pfam (PF12861) In PDB | Homo sapiens (Human) | APC11,Cyclosome subunit 11,Hepatocellular carcinoma-associated RING finger protein |
3 | C, P | Cell division cycle protein 23 homolog | polymer | 597 | 69075.1 | 2 | UniProt (Q9UJX2) Pfam (PF04049) In PDB | Homo sapiens (Human) | Anaphase-promoting complex subunit 8,APC8,Cyclosome subunit 8 |
4 | E | Anaphase-promoting complex subunit 16 | polymer | 110 | 11678.0 | 1 | UniProt (Q96DE5) Pfam (PF17256) In PDB | Homo sapiens (Human) | APC16,Cyclosome subunit 16 |
5 | F, H | Cell division cycle protein 27 homolog | polymer | 824 | 92519.5 | 2 | UniProt (P30260) Pfam (PF00515) Pfam (PF12895) In PDB | Homo sapiens (Human) | Anaphase-promoting complex subunit 3,APC3,CDC27 homolog,CDC27Hs,H-NUC |
6 | G, W | Anaphase-promoting complex subunit CDC26 | polymer | 85 | 9920.1 | 2 | UniProt (Q8NHZ8) Pfam (PF10471) In PDB | Homo sapiens (Human) | Anaphase-promoting complex subunit 12,APC12,Cell division cycle protein 26 homolog |
7 | I | Anaphase-promoting complex subunit 4 | polymer | 808 | 92303.3 | 1 | UniProt (Q9UJX5) Pfam (PF12894) Pfam (PF12896) In PDB | Homo sapiens (Human) | APC4,Cyclosome subunit 4 |
8 | J, K | Cell division cycle protein 16 homolog | polymer | 620 | 71929.7 | 2 | UniProt (Q13042) Pfam (PF12895) Pfam (PF13424) In PDB | Homo sapiens (Human) | Anaphase-promoting complex subunit 6,APC6,CDC16 homolog,CDC16Hs,Cyclosome subunit 6 |
9 | L | Anaphase-promoting complex subunit 10 | polymer | 185 | 21310.2 | 1 | UniProt (Q9UM13) Pfam (PF03256) In PDB | Homo sapiens (Human) | APC10,Cyclosome subunit 10 |
10 | M | Anaphase-promoting complex subunit 13 | polymer | 74 | 8528.3 | 1 | UniProt (Q9BS18) Pfam (PF05839) In PDB | Homo sapiens (Human) | APC13,Cyclosome subunit 13 |
11 | N | Anaphase-promoting complex subunit 2 | polymer | 822 | 94149.2 | 1 | UniProt (Q9UJX6) Pfam (PF00888) Pfam (PF08672) In PDB | Homo sapiens (Human) | APC2,Cyclosome subunit 2 |
12 | O | Anaphase-promoting complex subunit 5 | polymer | 755 | 85446.0 | 1 | UniProt (Q9UJX4) Pfam (PF21371) Pfam (PF12862) In PDB | Homo sapiens (Human) | APC5,Cyclosome subunit 5 |
13 | Q | Mitotic checkpoint serine/threonine-protein kinase BUB1 beta | polymer | 1050 | 120004.2 | 1 | UniProt (O60566) Pfam (PF08311) In PDB | Homo sapiens (Human) | MAD3/BUB1-related protein kinase,hBUBR1,Mitotic checkpoint kinase MAD3L,Protein SSK1 |
14 | R, S | Cell division cycle protein 20 homolog | polymer | 499 | 54796.5 | 2 | UniProt (Q12834) Pfam (PF12894) Pfam (PF00400) In PDB | Homo sapiens (Human) | p55CDC |
15 | T | Mitotic spindle assembly checkpoint protein MAD2A | polymer | 205 | 23533.9 | 1 | UniProt (Q13257) Pfam (PF02301) In PDB | Homo sapiens (Human) | HsMAD2,Mitotic arrest deficient 2-like protein 1,MAD2-like protein 1 |
16 | U | unknown | polymer | 9 | 785.9 | 1 | Homo sapiens (Human) | ||
17 | X, Y | Anaphase-promoting complex subunit 7 | polymer | 565 | 63386.2 | 2 | UniProt (Q9UJX3) Pfam (PF13181) In PDB | Homo sapiens (Human) | APC7,Cyclosome subunit 7 |
Sequence modifications
A: 1 - 1944 (UniProt: Q9H1A4)
C, P: 1 - 597 (UniProt: Q9UJX2)
F, H: 1 - 824 (UniProt: P30260)
G, W: 1 - 85 (UniProt: Q8NHZ8)
I: 1 - 808 (UniProt: Q9UJX5)
J, K: 1 - 620 (UniProt: Q13042)
L: 1 - 184 (UniProt: Q9UM13)
N: 1 - 822 (UniProt: Q9UJX6)
O: 1 - 755 (UniProt: Q9UJX4)
Q: 1 - 1050 (UniProt: O60566)
X, Y: 35 - 599 (UniProt: Q9UJX3)
PDB | External Database | Details |
---|---|---|
Glu 202 | Ser 202 | engineered mutation |
Glu 286 | Ser 286 | engineered mutation |
Glu 291 | Thr 291 | engineered mutation |
Glu 313 | Ser 313 | engineered mutation |
Glu 316 | Thr 316 | engineered mutation |
Glu 317 | Ser 317 | engineered mutation |
Glu 334 | Ser 334 | engineered mutation |
Glu 341 | Ser 341 | engineered mutation |
Glu 343 | Ser 343 | engineered mutation |
Glu 355 | Ser 355 | engineered mutation |
Glu 362 | Ser 362 | engineered mutation |
Glu 372 | Ser 372 | engineered mutation |
Glu 377 | Ser 377 | engineered mutation |
Glu | Thr 537 | engineered mutation |
Glu | Ser 547 | engineered mutation |
Glu | Ser 555 | engineered mutation |
Glu | Ser 569 | engineered mutation |
Gln 671 | Asn 671 | conflict |
Glu | Ser 688 | engineered mutation |
Glu | Ser 699 | engineered mutation |
Glu 916 | Ser 916 | engineered mutation |
Glu 1347 | Ser 1347 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 542 | Thr 542 | engineered mutation |
Glu 562 | Thr 562 | engineered mutation |
Glu 582 | Thr 582 | engineered mutation |
Glu 588 | Ser 588 | engineered mutation |
Glu 596 | Thr 596 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 200 | Thr 200 | engineered mutation |
Glu 205 | Thr 205 | engineered mutation |
Glu 220 | Ser 220 | engineered mutation |
Glu 241 | Ser 241 | engineered mutation |
Glu 276 | Ser 276 | engineered mutation |
Glu 320 | Ser 320 | engineered mutation |
Glu 336 | Ser 336 | engineered mutation |
Glu 339 | Ser 339 | engineered mutation |
Glu 386 | Ser 386 | engineered mutation |
Glu 387 | Ser 387 | engineered mutation |
Glu 393 | Ser 393 | engineered mutation |
Glu 426 | Ser 426 | engineered mutation |
Glu 435 | Ser 435 | engineered mutation |
Glu 446 | Thr 446 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 51 | Ser 51 | engineered mutation |
Glu 52 | Ser 52 | engineered mutation |
Glu 82 | Ser 82 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 777 | Ser 777 | engineered mutation |
Glu 779 | Ser 779 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 112 | Ser 112 | engineered mutation |
Glu 560 | Ser 560 | engineered mutation |
Glu 581 | Thr 581 | engineered mutation |
Glu 585 | Thr 585 | engineered mutation |
Glu 586 | Ser 586 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 3 | Thr 3 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 218 | Ser 218 | engineered mutation |
Glu 314 | Ser 314 | engineered mutation |
Glu 470 | Ser 470 | engineered mutation |
Glu 534 | Ser 534 | engineered mutation |
Glu 811 | Ser 811 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 178 | Thr 178 | engineered mutation |
Glu 179 | Ser 179 | engineered mutation |
Glu 195 | Ser 195 | engineered mutation |
Glu 202 | Ser 202 | engineered mutation |
Glu 221 | Ser 221 | engineered mutation |
Glu 232 | Thr 232 | engineered mutation |
Glu 364 | Ser 364 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 367 | Ser 367 | engineered mutation |
Glu 435 | Ser 435 | engineered mutation |
Glu 543 | Ser 543 | engineered mutation |
Glu 600 | Thr 600 | engineered mutation |
Glu 665 | Ser 665 | engineered mutation |
Glu 670 | Ser 670 | engineered mutation |
Glu 720 | Ser 720 | engineered mutation |
Glu 1043 | Ser 1043 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Glu 119 | Ser 119 | engineered mutation |
Glu 120 | Thr 120 | engineered mutation |
Glu 123 | Ser 123 | engineered mutation |
Glu 125 | Ser 125 | engineered mutation |
Glu 126 | Thr 126 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 23 |
Total formula weight | 1408427.9 | |
All* | Total formula weight | 1408427.9 |