1KI1: G25K GTP-binding protein, placental isoform

Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42. Determined by X-ray diffraction at 2.3 Å resolution. Released 29 May 2002.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,565
Mol. weight: 123.95 kDa
Released: 29 May 2002

Explore 1KI1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KI1 contains 50 α-helices and 38 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and C: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
α-helix	16-25	10
β-strand	40-46	7	1
β-strand	49-56	8	1
α-helix	68-71	4
β-strand	77-83	7	1
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	1
α-helix	117-119	3
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
β-strand	153-156	4	1
α-helix	165-177	13

Chains B and D: 15 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	1233-1259	27
α-helix	1260-1264	5
α-helix	1265-1270	6
α-helix	1275-1282	8
α-helix	1285-1306	22
α-helix	1316-1322	7
α-helix	1323-1326	4
α-helix	1328-1349	22
α-helix	1351-1361	11
α-helix	1364-1366	3
α-helix	1371-1374	4
α-helix	1377-1393	17
α-helix	1403-1437	35
β-strand	1440-1441	2	2
β-strand	1454	1	3
β-strand	1460	1	3
β-strand	1463-1466	4	2
β-strand	1470	1	4
β-strand	1479-1483	5	2
β-strand	1486-1493	8	2
β-strand	1511-1514	4	2
β-strand	1519-1520	2	2
α-helix	1521-1523	3
β-strand	1524-1527	4	5
β-strand	1540-1543	4	5
β-strand	1546-1549	4	5
β-strand	1551	1	4
α-helix	1555-1576	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G25K GTP-binding protein, placental isoform	A, C	protein	188	Homo sapiens	P60953 (AlphaFold model)
intersectin long form	B, D	protein	352	Homo sapiens	Q15811 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1KI1_1 G25K GTP-binding protein, placental isoform (chains A, C)
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP
EPKKSRRS

Sequence of entity 2 (B, D), FASTA

>1KI1_2 intersectin long form (chains B, D)
DMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAMIFVNWKEL
IMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSRQLNGAALIQQKTD
EAPDFKEFVKRLEMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKH
ALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQLVFNSVTNCLGPRKFLHSGK
LYKAKNNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYMYKTPIFLNEVLVKL
PTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKR

Primary citation

Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Snyder, J.T., Worthylake, D.K., Rossman, K.L. et al. Nat Struct Biol (2002) 9:468-475. DOI 10.1038/nsb796 · PubMed

Other PDB entries of the same protein (UniProt P60953 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2NGR 1.9 Å, Transition state complex for GTP hydrolysis by CDC42: comparisons of the high resolution…
4JS0 1.9 Å, Complex of Cdc42 with the CRIB-PR domain of IRSp53
6SUP 2.0 Å, Crystal Structure of TcdB2-TccC3-Cdc42
3VHL 2.08 Å, Crystal structure of the DHR-2 domain of DOCK8 in complex with Cdc42 (T17N mutant)
1GRN 2.1 Å, Crystal structure of the CDC42/CDC42GAP/ALF3 complex.
1NF3 2.1 Å, Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity…
2DFK 2.15 Å, Crystal structure of the CDC42-Collybistin II complex
2WM9 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
2WMO 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
1GZS 2.3 Å, Crystal structure of the complex between the gef domain of the salmonella typhimurium…
3GCG 2.3 Å, crystal structure of MAP and CDC42 complex
4ITR 2.3 Å, Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42

Browse structure collections

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