1CVI: Human prostatic acid phosphatase

Crystal structure of human prostatic acid phosphatase. Determined by X-ray diffraction at 3.2 Å resolution. Released 31 Aug 1999.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 12,376
Mol. weight: 167.2 kDa
Ligands: NAG, GLY
Released: 31 Aug 1999

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

Secondary structure: helices and β-sheets

1CVI contains 97 α-helices and 40 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: 25 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	1002-1011	10	1
β-strand	1015	1	2
α-helix	1028-1030	3
α-helix	1037	1
β-strand	1038	1	2
α-helix	1039	1
α-helix	1040-1056	17
β-strand	1070-1075	6	1
α-helix	1078-1091	14
α-helix	1096-1098	3
β-strand	1112-1114	3	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	1220-1224	5
α-helix	1229-1244	16
β-strand	1251-1256	6	1
α-helix	1258-1267	10
β-strand	1281-1289	9	1
β-strand	1292-1300	9	1
α-helix	1306-1307	2
β-strand	1308-1309	2	1
α-helix	1310	1
β-strand	1318-1320	3	1
α-helix	1321-1328	8
α-helix	1329-1331	3
α-helix	1336-1340	5

Chain B: 24 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	2002-2011	10	3
β-strand	2015	1	4
α-helix	2028-2030	3
α-helix	2037	1
β-strand	2038	1	4
α-helix	2039	1
α-helix	2040-2056	17
β-strand	2070-2075	6	3
α-helix	2078-2091	14
α-helix	2096-2098	3
β-strand	2112-2114	3	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	2220-2224	5
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	2308-2309	2	3
α-helix	2310	1
β-strand	2318-2320	3	3
α-helix	2321-2328	8
α-helix	2336-2340	5

Chain C: 24 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	3002-3011	10	5
β-strand	3015	1	6
α-helix	3028-3030	3
α-helix	3037	1
β-strand	3038	1	6
α-helix	3039	1
α-helix	3040-3056	17
β-strand	3070-3075	6	5
α-helix	3078-3091	14
α-helix	3096-3098	3
β-strand	3112-3114	3	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	3220-3224	5
α-helix	3229-3244	16
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	3308-3309	2	5
α-helix	3310	1
β-strand	3318-3320	3	5
α-helix	3321-3328	8
α-helix	3336-3340	5

Chain D: 24 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4002-4011	10	7
β-strand	4015	1	8
α-helix	4028-4030	3
α-helix	4037	1
β-strand	4038	1	8
α-helix	4039	1
α-helix	4040-4056	17
β-strand	4070-4075	6	7
α-helix	4078-4091	14
α-helix	4096-4098	3
β-strand	4112-4114	3	7
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	4220-4224	5
α-helix	4229-4244	16
β-strand	4251-4256	6	7
α-helix	4258-4267	10
β-strand	4281-4289	9	7
β-strand	4292-4300	9	7
α-helix	4306-4307	2
β-strand	4308-4309	2	7
α-helix	4310	1
β-strand	4318-4320	3	7
α-helix	4321-4328	8
α-helix	4329-4331	3
α-helix	4336-4340	5

Molecules and chains

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

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

>1CVI_1 PROSTATIC 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	3
GLY	Glycine	C2 H5 N O2	4

Primary citation

Crystal structure of human prostatic acid phosphatase . Jakob, C.G., Lewinski, K., Kuciel, R. et al. Prostate (2000) 42:211-218. DOI 10.1002/(SICI)1097-0045(20000215)42:3<211::AID-PROS7>3.0.CO;2-U · 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…
2HPA 2.9 Å, Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase
8XJ4 3.19 Å, Structure of prostatic acid phosphatase in human semen
2L3H NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the…

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