2HPA: Protein

Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. Determined by X-ray diffraction at 2.9 Å resolution. Released 16 Sept 1998.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 11,766
Mol. weight: 162.34 kDa
Ligands: NAG, PT3
Released: 16 Sept 1998

Explore 2HPA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HPA contains 87 α-helices and 44 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.

Chain A: 22 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	1003-1011	9	1
β-strand	1015	1	2
α-helix	1028-1030	3
β-strand	1038	1	2
α-helix	1040-1056	17
β-strand	1070-1074	5	1
α-helix	1078-1091	14
α-helix	1096-1098	3
β-strand	1112	1	1
α-helix	1116-1118	3
α-helix	1124	1
α-helix	1126	1
α-helix	1130-1141	12
α-helix	1143-1149	7
α-helix	1150-1152	3
α-helix	1153-1163	11
α-helix	1170-1172	3
α-helix	1173-1178	6
α-helix	1179-1186	8
α-helix	1197-1215	19
α-helix	1220-1225	6
α-helix	1229-1244	16
β-strand	1251-1256	6	1
α-helix	1258-1268	11
β-strand	1281-1289	9	1
β-strand	1292-1300	9	1
α-helix	1306-1309	4
β-strand	1310	1	1
β-strand	1319-1320	2	1
α-helix	1321-1328	8
α-helix	1329-1331	3
α-helix	1336-1340	5

Chain B: 22 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	2002-2011	10	3
β-strand	2015	1	4
α-helix	2028-2030	3
β-strand	2038	1	4
α-helix	2040-2056	17
β-strand	2070-2074	5	3
α-helix	2078-2091	14
α-helix	2096-2098	3
β-strand	2111-2112	2	3
α-helix	2116-2118	3
α-helix	2124	1
α-helix	2126	1
α-helix	2130-2141	12
α-helix	2143-2149	7
α-helix	2150-2152	3
α-helix	2153-2163	11
α-helix	2170-2172	3
α-helix	2173-2178	6
α-helix	2179-2186	8
α-helix	2197-2215	19
α-helix	2220-2226	7
α-helix	2229-2244	16
β-strand	2251-2256	6	3
α-helix	2258-2268	11
β-strand	2281-2289	9	3
β-strand	2292-2300	9	3
α-helix	2306-2307	2
β-strand	2308-2310	3	3
β-strand	2318-2320	3	3
α-helix	2321-2328	8
α-helix	2329-2331	3
α-helix	2336-2340	5

Chain C: 22 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3003-3011	9	5
β-strand	3015	1	6
α-helix	3028-3030	3
β-strand	3032	1	7
β-strand	3034	1	7
β-strand	3038	1	6
α-helix	3040-3056	17
β-strand	3070-3074	5	5
α-helix	3078-3091	14
α-helix	3096-3098	3
β-strand	3111-3112	2	5
α-helix	3116-3118	3
α-helix	3124	1
α-helix	3126	1
α-helix	3130-3141	12
α-helix	3143-3149	7
α-helix	3150-3152	3
α-helix	3153-3163	11
α-helix	3170-3172	3
α-helix	3173-3178	6
α-helix	3179-3186	8
α-helix	3197-3215	19
α-helix	3220-3226	7
α-helix	3228-3244	17
β-strand	3251-3256	6	5
α-helix	3258-3268	11
β-strand	3281-3289	9	5
β-strand	3292-3300	9	5
α-helix	3306-3307	2
β-strand	3308-3310	3	5
β-strand	3319-3320	2	5
α-helix	3321-3328	8
α-helix	3329-3331	3
α-helix	3336-3340	5

Chain D: 21 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	4003-4011	9	8
β-strand	4015	1	9
α-helix	4028-4030	3
β-strand	4032	1	10
β-strand	4034	1	10
β-strand	4038	1	9
α-helix	4040-4056	17
β-strand	4070-4074	5	8
α-helix	4078-4091	14
α-helix	4096-4098	3
β-strand	4111-4112	2	8
α-helix	4116-4118	3
α-helix	4124	1
α-helix	4126	1
α-helix	4130-4141	12
α-helix	4143-4149	7
α-helix	4150-4152	3
α-helix	4153-4163	11
α-helix	4170-4172	3
α-helix	4173-4178	6
α-helix	4179-4186	8
α-helix	4197-4215	19
α-helix	4220-4226	7
α-helix	4228-4244	17
β-strand	4251-4256	6	8
α-helix	4258-4268	11
β-strand	4281-4289	9	8
β-strand	4292-4300	9	8
β-strand	4308-4310	3	8
β-strand	4319-4320	2	8
α-helix	4321-4327	7
α-helix	4329-4331	3
α-helix	4336-4340	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (acid phosphatase)	A, B, C, D	protein	342	Homo sapiens	P15309 (AlphaFold model)

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

>2HPA_1 PROTEIN (ACID PHOSPHATASE) (chains A, B, C, D)
KELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKF
LNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQ
LLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDP
LYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMK
RATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYR
NETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMT

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5
PT3	N-propyl-tartramic acid	C7 H13 N O5	3

Primary citation

Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. LaCount, M.W., Handy, G., Lebioda, L. J Biol Chem (1998) 273:30406-30409. DOI 10.1074/jbc.273.46.30406 · PubMed

Other PDB entries of the same protein (UniProt P15309 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3PPD 1.5 Å, GGVLVN segment from Human Prostatic Acid Phosphatase Residues 260-265, involved in…
9NMV 1.97 Å, TCR156 S32Halpha bound to HLA A*02:01-PAP
9NMY 2.01 Å, TCR156 S32Qalpha bound to HLA A*02:01-PAP
9NMU 2.1 Å, TCR156 bound to HLA A*02:01-PAP
9NMW 2.11 Å, TCR156 S30Ealpha S32Qalpha bound to HLA A*02:01-PAP
9NMX 2.19 Å, TCR156 S32Malpha variant bound to HLA A*02:01-PAP
1ND6 2.4 Å, Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion…
9YTD 2.5 Å, Designed antibody vAB66 targeting PAP-HLA A*02:01
1ND5 2.9 Å, Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion…
8XJ4 3.19 Å, Structure of prostatic acid phosphatase in human semen
1CVI 3.2 Å, Crystal structure of human prostatic acid phosphatase
2L3H NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the…

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