Structure for peptidase M14.001: carboxypeptidase A1

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

PDB	Organism	Resolution	Comment
1PCA	Sus scrofa	2.00 Å	precursor
The catalytic zinc is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His69 and His196 in purple, and Glu72 in dark blue. The propeptide is shown in grey.

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3CPA	Bos taurus	2.00 Å	complex with glycyl-L-tyrosine
The catalytic zinc is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His179 and His306 in purple, and Glu182 in dark blue. The substrate-binding residues are shown in ball-and-stick representation in white: Arg71, Asn144, Arg145, Tyr198 and Tyr247. Glycyl-L-tyrosine is shown in grey in ball-and-stick representation.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Bos taurus
complex with Gly-L-Tyr	1.60 Å	0CPS	0CPS	0CPS	0CPS	0CPS	0CPS
zinc removed	1.86 Å	1ARL	1ARL	1ARL	1ARL	1ARL	1ARL	Greenblatt et al., 1998
zinc replaced with mercury	1.74 Å	1ARM	1ARM	1ARM	1ARM	1ARM	1ARM	Greenblatt et al., 1998
complex with 2-benzyl-3-iodo-propanoic acid	1.60 Å	1BAV	1BAV	1BAV	1BAV	1BAV	1BAV	Massova et al., 1996
complex with L-benzylsuccinate inhibitor	2.00 Å	1CBX	1CBX	1CBX	1CBX	1CBX	1CBX	Mangani et al., 1992
complex with [L-2-carboxy-3-phenylpropyl]methyl-sulfodiimine	2.25 Å	1CPS	1CPS	1CPS	1CPS	1CPS	1CPS	Cappalonga et al., 1992
beta form with two zinc ions in active site	2.00 Å	1CPX	1CPX	1CPX	1CPX	1CPX	1CPX	Bukrinsky et al., 1998
cadmium-substituted form at pH 7.5	1.70 Å	1EE3	1EE3	1EE3	1EE3	1EE3	1EE3	Jensen et al., 2002
cadmium-substituted form at pH 7.5	1.76 Å	1ELL	1ELL	1ELL	1ELL	1ELL	1ELL	Jensen et al., 2002
cadmium-substituted form at pH 5.5	2.00 Å	1ELM	1ELM	1ELM	1ELM	1ELM	1ELM	Jensen et al., 2002
complex with D-cysteine	1.75 Å	1F57	1F57	1F57	1F57	1F57	1F57	van et al., 2000
complex with D-N-hydroxyaminocarbonyl-Phe	2.30 Å	1HDQ	1HDQ	1HDQ	1HDQ	1HDQ	1HDQ	Cho et al., 2002
complex with aminocarbonyl-Phe	1.75 Å	1HDU	1HDU	1HDU	1HDU	1HDU	1HDU	Cho et al., 2002
complex with L-N-hydroxyaminocarbonyl-Phe	1.75 Å	1HEE	1HEE	1HEE	1HEE	1HEE	1HEE	Cho et al., 2002
complex with phenylalanine-N-sulfonamide	2.00 Å	1IY7	1IY7	1IY7	1IY7	1IY7	1IY7	Park et al., 2002
mature peptidase	1.25 Å	1M4L	1M4L	1M4L	1M4L	1M4L	1M4L	Kilshtain-Vardi et al., 2003
complex of procarboxypeptidase A, proproteinase E and chymotrypsinogen C	2.35 Å	1PYT	1PYT	1PYT	1PYT	1PYT	1PYT	Gomis-Ruth et al., 1995
mature peptidase	1.53 Å	1YME	1YME	1YME	1YME	1YME	1YME	Greenblatt et al., 1998
complex with tick carboxypeptidase inhibitor	1.70 Å	1ZLH	1ZLH	1ZLH	1ZLH	1ZLH	1ZLH	Arolas et al., 2005
complex with engineered leech metallocarboxypeptidase inhibitor	2.16 Å	2ABZ	2ABZ	2ABZ	2ABZ	2ABZ	2ABZ	Arolas et al., 2005
mature peptidase	1.50 Å	2CTB	2CTB	2CTB	2CTB	2CTB	2CTB	Teplyakov et al., 1993
complex with L-phenyl lactate	1.40 Å	2CTC	2CTC	2CTC	2CTC	2CTC	2CTC	Teplyakov et al., 1993
crystal structure analysis of cpa-2-benzyl-3-nitropropanoic acid complex	1.70 Å	2RFH	2RFH	2RFH	2RFH	2RFH	2RFH	Wang et al., 2008
complex with glycyl-L-tyrosine	2.00 Å	3CPA	3CPA	3CPA	3CPA	3CPA	3CPA	Christianson & Lipscomb, 1986
crystallogic studies on the complex of carboxypeptidase a with inhibitors using alpha-hydroxy ketone as zinc-binding group	1.85 Å	3FVL	3FVL	3FVL	3FVL	3FVL	3FVL
x-ray crystallographic studies on the complex of carboxypeptidase a with the inhibitor using alpha-nitro ketone as the zinc-binding group	1.85 Å	3FX6	3FX6	3FX6	3FX6	3FX6	3FX6
complex with an organic small-molecule: conformational changes	1.60 Å	3HLP	3HLP	3HLP	3HLP	3HLP	3HLP
complex with an organic small-molecule: conformational changes	1.90 Å	3HUV	3HUV	3HUV	3HUV	3HUV	3HUV
complex with a thiirane mechanism-based inactivator	1.39 Å	3I1U	3I1U	3I1U	3I1U	3I1U	3I1U
complex with an organic small-molecule: conformational changes	1.70 Å	3KGQ	3KGQ	3KGQ	3KGQ	3KGQ	3KGQ
complex with potato carboxypeptidase A inhibitor	2.50 Å	4CPA	4CPA	4CPA	4CPA	4CPA	4CPA	Rees & Lipscomb, 1982
mature peptidase	1.54 Å	5CPA	5CPA	5CPA	5CPA	5CPA	5CPA	Rees et al., 1983
complex with O-[[(1R)-[[N-phenylmethoxycarbonyl)-L-Ala]amino]ethyl]hydroxyphosphinyl]-L-3-phenyllactate	2.00 Å	6CPA	6CPA	6CPA	6CPA	6CPA	6CPA	Kim & Lipscomb, 1990
complex with Bz-Phe-Val-P-(O)-Phe	2.00 Å	7CPA	7CPA	7CPA	7CPA	7CPA	7CPA	Kim & Lipscomb, 1991
complex with BZ-Ala-Gly-(P)-(O)-Phe	2.00 Å	8CPA	8CPA	8CPA	8CPA	8CPA	8CPA	Kim & Lipscomb, 1991
Homo sapiens
mature peptidase	1.60 Å	2V77	2V77	2V77	2V77	2V77	2V77	Pallares et al., 2008
complex with carboxypeptidase A inhibitor (Ascaris suum)	1.60 Å	3FJU	3FJU	3FJU	3FJU	3FJU	3FJU	Sanglas et al., 2009
complex with the phosphinic inhibitor acetyl-leu-ala-y(po2ch2)-homophe-oh	2.27 Å	4UEE	4UEE	4UEE	4UEE	4UEE	4UEE
complex with the phosphinic inhibitor acetyl-tyr-ala-y(po2ch2)-homophe-oh	1.69 Å	4UEF	4UEF	4UEF	4UEF	4UEF	4UEF
complex with the phosphinic inhibitor acetyl-leu-phe-y( po2ch2)-phe-oh	2.29 Å	4UEZ	4UEZ	4UEZ	4UEZ	4UEZ	4UEZ
complex with a thiirane mechanism-based inhibitor	1.77 Å	4UF4	4UF4	4UF4	4UF4	4UF4	4UF4
complex with a thiirane mechanism-based inhibitor	1.80 Å	5OM9	5OM9	5OM9	5OM9	5OM9	5OM9
complex with thephosphinic inhibitor acetyl-tyr-ala-y(po2ch2)-homophe-oh	1.72 Å	6I6Z	6I6Z	6I6Z	6I6Z	6I6Z	6I6Z
Sus scrofa
precursor	2.00 Å	1PCA	1PCA	1PCA	1PCA	1PCA	1PCA	Guasch et al., 1992