5MAV: Human PCNA

Crystal structure of human PCNA in complex with PARG (poly(ADP-ribose) glycohydrolase) peptide. Determined by X-ray diffraction at 2.58 Å resolution. Released 2 Aug 2017.

Method: X-ray diffraction
Resolution: 2.58 Å
Organism: Homo sapiens
Chains: 12
Atoms: 12,192
Mol. weight: 187.59 kDa
Released: 2 Aug 2017

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

Secondary structure: helices and β-sheets

5MAV contains 48 α-helices and 133 β-strands across 12 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: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
α-helix	10-20	11
β-strand	25-31	7	2
β-strand	34-40	7	2
β-strand	46-53	8	2
α-helix	54-56	3
β-strand	59-62	4	1
β-strand	66-71	6	2
α-helix	72-80	9
α-helix	86	1
β-strand	87-92	6	1
β-strand	98-104	7	1
β-strand	110-117	8	1
β-strand	119	1	2
β-strand	126-127	2	3
β-strand	135-140	6	2
α-helix	141-154	14
β-strand	157-162	6	4
β-strand	166-173	8	4
β-strand	176-183	8	4
β-strand	196-199	4	2
β-strand	203-208	6	4
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	2
β-strand	235-241	7	2
β-strand	245-251	7	2
β-strand	254	1	5

Chain B: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	12
α-helix	10-20	11
β-strand	25-30	6	13
β-strand	34-35	2	13
β-strand	38-40	3	13
β-strand	46-53	8	13
α-helix	54-56	3
β-strand	59-62	4	12
β-strand	66-71	6	13
α-helix	72-80	9
α-helix	86	1
β-strand	87-92	6	12
β-strand	98-104	7	12
β-strand	110-117	8	12
β-strand	126	1	14
β-strand	135-140	6	13
α-helix	141-154	14
β-strand	157-162	6	15
β-strand	166-173	8	15
β-strand	176-183	8	15
β-strand	196-199	4	13
β-strand	203-208	6	15
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	13
β-strand	235-241	7	13
β-strand	245-251	7	13
β-strand	254	1	16

Chain C: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	6
α-helix	10-17	8
β-strand	25-30	6	7
β-strand	34-40	7	7
β-strand	46-53	8	7
α-helix	54-56	3
β-strand	59-62	4	6
β-strand	66-71	6	7
α-helix	72-80	9
β-strand	87-92	6	6
β-strand	98-104	7	6
β-strand	110-117	8	6
β-strand	119	1	7
β-strand	126	1	8
β-strand	135-140	6	7
α-helix	141-154	14
β-strand	157-162	6	1
β-strand	166-173	8	1
β-strand	176-183	8	1
β-strand	196-199	4	7
β-strand	203-208	6	1
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	7
β-strand	235-241	7	7
β-strand	245-251	7	7
β-strand	254	1	9

Chain D: 6 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	17
α-helix	10-20	11
β-strand	25-30	6	18
β-strand	34-39	6	18
β-strand	46-53	8	18
α-helix	54-56	3
β-strand	59-60	2	17
β-strand	66-71	6	18
α-helix	72-79	8
β-strand	87-90	4	17
β-strand	99-104	6	17
β-strand	110-116	7	17
β-strand	119	1	18
β-strand	135-140	6	18
α-helix	141-154	14
β-strand	157-162	6	12
β-strand	166-173	8	12
β-strand	176-183	8	12
β-strand	196-199	4	18
β-strand	203-208	6	12
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	18
β-strand	235-241	7	18
β-strand	245-251	7	18
β-strand	254	1	19

Chain E: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	4
α-helix	10-20	11
β-strand	25-30	6	10
β-strand	34-40	7	10
β-strand	46-53	8	10
β-strand	59-62	4	4
β-strand	66-71	6	10
α-helix	72-80	9
β-strand	87-92	6	4
β-strand	98-104	7	4
β-strand	111-117	7	4
β-strand	126	1	11
β-strand	135-140	6	10
α-helix	141-151	11
β-strand	157-163	7	6
β-strand	166-173	8	6
β-strand	176-183	8	6
β-strand	196-199	4	10
β-strand	203-208	6	6
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	10
β-strand	235-241	7	10
β-strand	245-251	7	10

Chain F: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	15
α-helix	10-19	10
β-strand	25-31	7	20
β-strand	34-40	7	20
β-strand	46-53	8	20
α-helix	54-56	3
β-strand	59-62	4	15
β-strand	66-71	6	20
α-helix	72-80	9
β-strand	87-92	6	15
β-strand	98-104	7	15
β-strand	110-117	8	15
β-strand	119	1	20
β-strand	127	1	21
β-strand	135-140	6	20
α-helix	141-152	12
β-strand	158-163	6	17
β-strand	166-172	7	17
β-strand	176-183	8	17
β-strand	196-199	4	20
β-strand	203-207	5	17
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-230	7	20
β-strand	233-241	9	20
β-strand	245-251	7	20
β-strand	254	1	22

Chain G: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	407	1	9
α-helix	408-409	2
α-helix	410-412	3
α-helix	415	1
β-strand	416	1	8
α-helix	417	1

Chain H: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	407	1	5
α-helix	408-409	2
α-helix	410-412	3
β-strand	415-416	2	3
α-helix	417	1

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proliferating cell nuclear antigen	A, B, C, D, E, F	protein	264	Homo sapiens	P12004 (AlphaFold model)
Poly (ADP-ribose) glycohydrolase	G, H, K, L, M, N	protein	19	Homo sapiens	Q0MQR4 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>5MAV_1 Proliferating cell nuclear antigen (chains A, B, C, D, E, F)
GPAMFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGF
DTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMK
LMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGN
GNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVV
EYKIADMGHLKYYLAPKIEDEEGS

Sequence of entity 2 (G, H, K, L, M, N), FASTA

>5MAV_2 Poly (ADP-ribose) glycohydrolase (chains G, H, K, L, M, N)
QHGKKDSKITDHFMRLPKA

Primary citation

A novel non-canonical PIP-box mediates PARG interaction with PCNA. Kaufmann, T., Grishkovskaya, I., Polyansky, A.A. et al. Nucleic Acids Res (2017) 45:9741-9759. DOI 10.1093/nar/gkx604 · PubMed

Other PDB entries of the same protein (UniProt P12004 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1U7B 1.88 Å, Crystal structure of hPCNA bound to residues 331-350 of the flap endonuclease-1 (FEN1)
8F5Q 1.9 Å, Crystal structure of human PCNA in complex with the PIP box of FBH1
9N3L 1.9 Å, Co-crystal structure of PCNA bound to HSP90alpha inhibitor, SNX2112
5E0U 1.93 Å, Human PCNA variant (S228I) complexed with p21 at 1.9 Angstroms
5MLO 1.96 Å, Crystal structure of human PCNA in complex with ZRANB3 PIP box peptide
4RJF 2.01 Å, Crystal structure of the human sliding clamp at 2.0 angstrom resolution
5E0V 2.07 Å, Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms
3VKX 2.1 Å, Structure of PCNA
6HVO 2.1 Å, Crystal structure of human PCNA in complex with three peptides of p12 subunit of human…
4ZTD 2.2 Å, Crystal Structure of Human PCNA in complex with a TRAIP peptide
5YCO 2.2 Å, Complex structure of PCNA with UHRF2
5MOM 2.27 Å, Crystal Structure of PCNA encoding the hypomorphic mutation S228I

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