5OB5: C-X-C motif chemokine 2

fAb complex with GroBeta. AbVance: increasing our knowledge of antibody structural space to enable faster and better decision-making in antibody drug discovery. Determined by X-ray diffraction at 1.65 Å resolution. Released 8 Nov 2017.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,685
Mol. weight: 54.63 kDa
Released: 8 Nov 2017

Explore 5OB5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5OB5 contains 21 α-helices and 49 β-strands across 3 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.

Chain A: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	20-22	3
β-strand	23-29	7	1
β-strand	32	1	2
β-strand	35	1	2
β-strand	39-44	6	1
β-strand	49-52	4	1
α-helix	57-67	11

Chain H: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	3
α-helix	7-9	3
β-strand	10-12	3	4
β-strand	18-25	8	3
α-helix	29-31	3
β-strand	33-39	7	4
β-strand	45-52	8	4
β-strand	58-60	3	4
β-strand	68-73	6	3
α-helix	74-76	3
β-strand	78-83	6	3
α-helix	88-90	3
β-strand	92-99	8	4
β-strand	106-109	4	4
β-strand	113-117	5	4
α-helix	121-122	2
β-strand	123	1	5
α-helix	124-125	2
β-strand	126-130	5	6
β-strand	137-138	2	6
β-strand	141-151	11	6
β-strand	152	1	5
β-strand	157-160	4	7
α-helix	161-163	3
β-strand	165	1	7
β-strand	169-171	3	6
α-helix	172-174	3
β-strand	175-176	2	6
β-strand	182-191	10	6
α-helix	192-194	3
β-strand	201-206	6	7
α-helix	207-209	3
β-strand	211-216	6	7

Chain L: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	8
β-strand	10-14	5	9
β-strand	19-25	7	8
β-strand	33-38	6	9
β-strand	45-49	5	9
β-strand	53-54	2	9
α-helix	55	1
β-strand	62-67	6	8
β-strand	70-75	6	8
α-helix	80-82	3
β-strand	84-90	7	9
α-helix	96	1
β-strand	97-98	2	9
β-strand	102-107	6	9
β-strand	111	1	10
α-helix	112-113	2
β-strand	114-118	5	11
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	11
β-strand	140	1	10
β-strand	145-150	6	12
β-strand	153-154	2	12
α-helix	155	1
β-strand	159-163	5	11
α-helix	164-167	4
β-strand	173-182	10	11
α-helix	183-187	5
β-strand	191-197	7	12
β-strand	205-210	6	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C-X-C motif chemokine 2	A	protein	63	Homo sapiens	P19875 (AlphaFold model)
fAb Heavy chain	H	protein	220	Homo sapiens
fAb Light chain	L	protein	213	Homo sapiens

Sequence of entity 1 (A), FASTA

>5OB5_1 C-X-C motif chemokine 2 (chains A)
ELRCQCLQTLQGIHLKNIQSVKVKSPGPHCAQTEVIATLKNGQKACLNPASPMVKKIIEK
MLK

Sequence of entity 2 (H), FASTA

>5OB5_2 fAb Heavy chain (chains H)
QVQLVQSGAEVKKPGASVKVSCKASGYTFTNYWIVWVRQAPGQGLEWMGDLYSGGGYTFY
SENFKGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARSGYDRTWFAHWGQGTLVTVSSA
STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG
LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK

Sequence of entity 3 (L), FASTA

>5OB5_3 fAb Light chain (chains L)
DIQMTQSPSSLSASVGDRVTITCQASQDIESYLSWYQQKPGKAPKLLIYYATRLADGVPS
RFSGSGSGQDYTLTISSLQPEDFATYYCLQHGESPPTFGQGTKLEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE

Primary citation

AbVance: increasing our knowledge of antibody structural space to enable faster and better decision-making in antibody drug discovery. Convery, M.A. To be published.

Other PDB entries of the same protein (UniProt P19875 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8XXH 2.8 Å, Structure of CXCR2 bound to CXCL2 (CXCR2-CXCL2-Go Full map)
8XVU 3.09 Å, Structure of CXCR2 bound to CXCL2 (Ligand-receptor focused map)
1QNK Truncated human GROB[5-73], NMR, 20 structures

Browse structure collections

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